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Results 1 - 6 of 6
EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.76-
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.76adopts a fold consisting of two beta-barrels made each of six anti-parallel beta-sheets. Crystallizes as a tetramer, which can be regarded as a dimer of dimers: two monomers in a dimer are oriented so that their active sites face each other, preventing the binding of large substrates. The hole in the middle of the tetramer is lined with hydrophobic residues. Contains four disulfide bridges between cysteine pairs 42-58, 136-201, 168-182 and 191-220. No X-ray structure of PR3 with a substrate in its active site available
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.76crystal structure of recombinant PR3. Overall fold consists of two beta-barrel domains. PR3 structure includes a disaccharide unit covalently attached to Asn159. PR3 substrate binding sites at S4 to S3'
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.76molecular dynamics simulations of PR3 anchored at three different phospholipid bilayers: dimyristoylphosphatidylcholine DMPC and dimyristoylphosphatidylglycerol DMPG, and an equimolar mixture of DMPC/DMPG. Basic residues R177, R186A, R186B, K187 and R222 interact via hydrogen bonds with the lipid headgroups to stabilize PR3 at the interfacial membrane region. Hydrophobic amino acids V163, F165, F166, I217, L223, and F224 insert into the hydrophobic core below the carbonyl groups of the bilayers and aromatic amino acids F165, F192, F215, W218, F224, and F227 contribute electrostatic interaction via cation-pi interactions with the choline groups of DMPC. PR3 presents all the characteristics of a peripheral membrane protein with an ability to bind negative phospholipids. The catalytic triad remains unperturbed by the presence of the membrane, the ligand binding sites are located in close proximity to the membrane and amino acids K99 and I217 interact significantly with the lipids
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.76Sap3 in a stable complex with pepstatin A and in the absence of an inhibitor, in the presence of Zn2+, to 1.9 and 2.2 A resolution. Inhibitor binding causes active site closure by the movement of a flap segment. Sap3 consists of the S2' binding site becoming channelshaped subsequent to the turn of the loop with residues 129–135
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.76to 2.2 A resolution
Results 1 - 6 of 6