3.2.1.4: cellulase

393578, 393597

crystals of recombinant native enzyme diffract to 2.1 A, crystals of seleno-L-methionine-containing protein diffract to 2.8 A, hanging-drop vapour-diffusion method, crystals belong to space group P4(3)2(1)2

663523

hanging drop vapor diffusion method at 20°C, crystal structure of Cel44A is solved at a resolution of 0.96 A.The crystal structures of E186Q mutant complexed with cellopentaose and cellohexaose are solved at 2.0 and 1.8 A resolution, respectively

680853

purified recombinant C-terminally truncated mutant enzyme CtCel9QDELTAc complexed with Tris, Tris + cellobiose, cellobiose + cellotriose, cellotriose, and cellotetraose, sitting drop vapor diffusion method, a drop consists of 0.0013 ml of protein solution and 0.0013 ml of reservoir solution containing 9-12% w/v PEG 3350, 15-20% v/v PEG 550MME, 30 mM NaBr, 30 mM NaF, and 30 mM NaI, and 0.1 M Tris, pH 8.5, with or without 10 mM cellooligosaccharides, equilibration against 0.2 ml reservoir solution, 22°C, X-ray diffraction structure determination analysis at resolutions 1.50, 1.70, 2.05, 2.05, and 1.75 A, respectively. In both the oligosaccharide-free and cellobiose-bound CtCel9QDELTAc structures, a Tris molecule is observed in the active site

Q9AJF8

750321

purified recombinant detagged enzyme in complex with G3 or G5f, sitting drop vapour diffuson method, mixing of 0.027 ml of 40 mg/ml protein in 20 mM Tris, pH 7.5, and 6.7 mM G3 or G5f, with 0.027 ml of reservoir solution containing 12% Tacsimate, pH 5.0, 18% or 20% PEG 3350, 2 mM manganese(II) acetate, respectively, and equilibration against 0.4 ml of reservoir solution, 20°C, 3 days, X-ray diffraction structure determination and analysis at 1.04 and 0.99 A resolution, respectively, modelling

Bacillus sp. (in: Bacteria)

A3DCJ4

749520

molecular docking studies reveal Glu116 and Glu204 as important for functional interaction with carboxymethylcellulose and show hydrogen bonding with Asp99, Glu116, Glu204 and hydrophobic interactions with Trp22, Val58, Tyr61, Phe101, Met118, Trp120, Pro129, Ile130, Thr160 and Phe206

Aspergillus niger

O74705

735455

enzyme structure analysis using small-angle X-ray scattering at 30 A resolution and homology modelling with the crystallographic model of the endoglucanase TfCel9A (PDB ID 1JS4), structure comparisons

Bacillus licheniformis

Q65JI9

749715

hanging-drop vapour diffusion method, 1.9 A resolution

656490

structure of chimera C10 in complex with crown ether. The structure of C10 adopts the same classical TIM barrel fold as the parental structures of CelA core and Cel5A. A Ca2+ ion is bound to the backbone oxygen of G130 and to the side chains of D168, D170 and N171 with an average distance of 2.3 A

Bacillus subtilis

P10475

737095

purified recombinant His-tagged CcCel6C unbound and in complex with 4-nitrophenyl beta-D-cellotrioside and cellobiose, hanging drop vapour diffusion method, mixing of 0.001 ml of 21.5 mg/ml containing protein solution with 0.001 ml of well solution containing 100 mM HEPES/KOH, pH 7.0, 30% PEG 8000, 150 mM magnesium acetate, soaking of crystals in 60 mM 4-nitrophenyl beta-D-cellotrioside for 2 h or 220 mM cellobiose for 5 min in well solution for complex formation, X-ray diffraction structure determination and analysis at 1.6 A, 1.4 A, and 1.2 A resolution, respectively

Coprinopsis cinerea

708491

molecular modeling of structure

2 entries

hanging-drop vapour-diffusion method

Fervidobacterium nodosum Rt17-B1

a single crystal of CMCax (Crystal I) is grown at 20°C by the hanging drop vapor diffusion method against a reservoir solution containing 100 mM sodium citrate buffer, pH 4.4, 15% (w/v) PEG 4,000, 3% (w/v) PEG 8,000, and 20 mM ammonium sulfate. Crystal belongs to the space group P6(1) with unit cell dimensions of a = b = 89.1 A and c = 94.2 A. Another crystal of larger size (Crystal II) is obtained under the above conditions but with the addition of 10 mM cellobiose. Prior to X-ray diffraction experiments, the crystal is rapidly soaked in reservoir solution supplemented with 20% (v/v) glycerol, and flash-cooled under a stream of nitrogen gas. The crystal diffracted to a resolution of 1.65 A

Komagataeibacter xylinus

682750

enzyme crystallizes spontaneously at pH 4.0 and 7°C

Melanocarpus albomyces

Q8J0K8

742405

hanging-drop vapor-diffusion method with phosphate plus CdCl2 as precipitant. Pyramid-like crystals are formed and the diffract X-rays beyond 2.2 A resolution. It belongs to the space group P2(1)2(1)2(1) with unit cell parameters of a = 62.5 A, b = 71.7 A and c = 88.6 A

Niallia circulans

654825

molecular modeling of the catalytic domain. The domain structurally belongs to the GH-A family

Penicillium crustosum

U6A8H3

744814

to 1.5 A resolution. Comparison between enzyme and other representative GH45 members

Phanerodontia chrysosporium

B3Y002

746488

homology modeling of structure. Active site residues are Asn156, Glu157, His227, Tyr229, and Glu268

Photobacterium panuliri

A0A0M4FQ56

744068

hanging drop vapour diffusion method, catalytic core domain, 1.8 A resolution, the space group is P2(1)2(1)2(1) with unit cell parameters a = 135.1 A, b = 78.4 A and c = 4.1 A

Pseudoalteromonas haloplanktis

654070

a truncated EGPf (EGPfDELTAN30) mutant lacking the proline and hydroxyl-residue rich region at the N-terminus is constructed, and its crystal structure is resolved at an atomic resolution of 1.07 A, hanging-drop vapor-diffusion method at 25°C

Q9V2T0

722276

crystallization of protein at pH 5.5. Crystal form has the symmetry of space group C2. Two molecules of the enzyme are observed in the asymmetric unit. Crystal packing is weak at pH 5.5 owing to two flexible interfaces between symmetry-related molecules. Comparison of the enzyme structures obtained at pH 9.0 and pH 5.5 reveals a significant conformational difference at the active centre and in the surface loops

E7FHY8, Q9V2T0

728922

ctrystallization at pH 5.5, to 1.7 A resolution. Space group C2, two molecules in the asymmetric unit. Comparison of structures obtained at pH 9.0 and pH 5.5 reveals a significant conformational difference at the active centre and in the surface loops

E7FHY8

743954

hanging-drop vapour-diffusion method at pH 5.5. Crystal form has the symmetry of space group C2. Two molecules of the enzyme are observed in the asymmetric unit. Comparison of the structures obtained at pH 9.0 and pH 5.5 reveals a significant conformational difference at the active centre and in the surface loops

E7FHY8, Q9V2T0

728922

hanging-drop vapour-diffusion method. Truncated enzyme (DELTAN30) without the proline- and hydroxyl-rich regions at the N-terminus is prepared and crystallized. Crystals are obtained using the hanging-drop vapour-diffusion method at 30°C. An X-ray diffraction data set is collected to 1.07 A resolution. The crystal belong to space group P2(1)2(1)2 with unit-cell parameters a = 58.01, b = 118.67, c = 46.76 A

E7FHY8

721230

hanging-drop vapor-diffusion method

746401

hanging-drop vapor-diffusion method. The crystals are obtained over a period of about 3 days at 22°C

724939

hanging-drop vapour diffusion method. The crystal of the enzymeligand complex is prepared from the truncated protein lacking five amino acid residues from both the N- and C-terminal ends. Crystal structures of mutants enzymes (E201A, E342A and Y299F) in the complex with either the substrate or product ligands

744265

purified enzyme mutants in complex with either the substrate or product ligands, hanging drop vapour diffusion method, 20 mg/ml protein in 50 mM Tris/HCl, pH 8.0, mixing of 0.0015 ml of both protein and reservoir solution, the latter contaning 1.5 M ammonium phosphate, and 0.1 M MES, pH 6.5, 22°C, 3 days, X-ray diffraction structure determination and analysis at 1.65-2.01 A resolution

717220

X-ray diffraction analysis of crystals of the wild-type full-length EGPh is unsuccessful, sitting-drop vapour-diffusion method

690256

catalytic domain of CelF cellulase in the presence of a newly synthesized cellulase inhibitor

393646

catalytic domain of endoglucanase A

393628

crystal strcuture of free native enzyme and its complex with cellobiose solved to 1.8 A and 2.0 A resolution

654619

vapor diffusion and microseeding techniques, crystallization of complexes between hemithio-cello-deca and dodecaoses and the inactive mutants E44Q and E55Q of cellulase Cel48F

Thermothelomyces thermophilus

P37698

681469

hanging-drop vapor-diffusion method at room temperature. Structure of the complex of the catalytic domain of endoglucanase Cel6A with a nonhydrolyzable substrate analogue that acts as an inhibitor, methylcellobiosyl-4-thio-beta-cellobioside determined at 1.5 A resolution, structure of mutant enzyme Y73S, structure of mutant enzyme Y73S in complex with methylcellobiosyl-4-thio-beta-cellobioside at 1.04 A resolution, structure of mutant enzyme Y73S in complex with cellotetrose at 1.64 A resolution

Thermobifida fusca

664071

homology modeling of structure

Thermochaetoides thermophila

V9PD44

746486

homology modeling of structure. Residues E234 and E344 display a catalytically important role

745087

structures of apoenzyme and in complex with cellobiose and cellotetraose, to 1.36-1.58 A resolution. The protein folds into two overall regions, one is a six-stranded beta-barrel, and the other one consists of several extended loops. Between the two regions lies the substrate-binding channel, which is an open cleft spanning across the protein surface. A continuous substrate-binding cleft from subsite -4 to +3 canbe identified

Thermothielavioides terrestris

G2QVH7

744816

free energy simulations and quantum mechanical/molecular mechanical potential at both 37°C and 85°C. The free energy barriers for glycosylation and deglycosylation are 22.5 and 24.5 kcal/mol at 85°C, respectively. The barrier for deglycosylation decreases with increasing temperature or as a result of the Y61G mutation, consistent with experimental observations. The transition state for glycosylation and deglycosylation is in an oxocarbonium state with the -1 glucose ring having an E3 envelop (or 4H3 half-chair) conformation. A stable moiety exists that may play a role in holding cellulose at the binding site with the correct orientation for the reaction even at 85°C

Q60032

735918

homology modeling of structure

G4FFR3

737085

mutants Y16G, Y61GG and Y61del in complex with substrate beta-glucan. Mutations at the Tyr61 site do not affect the overall protein structure, but local perturbations might diminish the substrate-binding strength

Q60032

729059

wild-type and mutant E134C free or in complex crystals with cellotetraose and cellobiose, sitting drop vapor diffusion method for the wild-type enzyme usage of a reservoir solution containing 0.1 M Bis-Tris, pH 5.5, 10% glycerol, and 15% PEG 3350, for the mutant E134C a reservoir solution containing 0.1 M ammonium sulfate, 0.1 M Bis-Tris, pH 5.5, 5% glycerol, and 18% PEG 3350 is used, addition of 10 mM cellobiose or cellotetraose, room temperature, 2 days, X-ray diffraction structure determination and analysis at 1.47-2.09 A resolution