Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.4.21.107: peptidase Do

This is an abbreviated version!
For detailed information about peptidase Do, go to the full flat file.

Word Map on EC 3.4.21.107

Reaction

acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-/-Val =

Synonyms

bacterial PQC factor, BB_0104, BCAL2829, CD630_32840, Deg1, DEG2, DEG5, DEG7, DEG8, Deg9, DegP, DegP protease, DegP/HtrA, DegQ, DegS, DepP9, Do, Do protease, HhoA, HhoB, high temperature requirement A, high temperature requirement A protease, high temperature requirement A1, high temperature requirement factor A, high-temperature requirement A, high-temperature requirement A protease, high-temperature requirement A-1, high-temperature requirement A1, high-temperature requirement A1 protease, high-temperature requirement factor A, HtrA, HtrA (DegP) protease, HtrA heat shock protease, HtrA protease, HTRA serine peptidase 1, HtrA-like protease, HtrA/DegP, HtrA1, HtrA2, HtrA3, HTRA4, MAL8P1.126, More, MucD, Nma111p, Omi/HtrA protease orthologue Ynm3p, protease do, protease Do-like 5, protease Do-like 8, PRSS11, S01.273, serine protease, serine protease HtrA, serine protease HtrA1, YNL123w

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.107 peptidase Do

Crystallization

Crystallization on EC 3.4.21.107 - peptidase Do

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Deg9 displays an octameric structure consisting of two tetrameric rings with distinct conformations. In model of substrate recognition, protease activation of one tetramer is mediated by en-bloc reorientation of the protease domains to open an entrance for the substrate in the opposite (inactive) tetramer
mutant S266A, to 2.6 A resolution. The protein trimer contains two calcium ions in a central channel, suggesting a link between photodamage control and calcium ions in chloroplasts. Protein contains no PDZ domain and the trimeric structure reveals a catalytic triad conformation where His147 in the alternative conformation is rotated anticlockwise by 120°, preventing formation of the His147-Asp188 hydrogen bond
mutant S292A, to 2.0 A resolution. Isoform Deg8 forms a hexamer in the crystals. The catalytic triad of Deg8 consists of His171, Asp214 and Ser292. In the Deg8 (S292A) structure the triad fails to form catalytically competent hydrogen bonds owing to the anticlockwise rotation of the chi1 angle of His171 by 120°. His171 can form a hydrogen bond to Gln272 of loop L3
modeling of 3D structure
-
a theoretical model of the three-dimensional structure of the LA loop as per the resting state of enzyme HtrA. hydrophobic interactions connect the LA loops of the hexamer and polar contacts between the LA', i.e. the LA loop on an opposite subunit, and L1 loops on opposite subunits. Disturbance of these interactions causes the stimulation of HtrA proteolytic activity. LA loops contribute to the preservation of the integrity of the HtrA oligomer and to the stability of the monomer
crystal structure of the DegP24 multimer-outer membrane protein complex is solved by the single-wavelength anomalous dispersion method: The 24-mer of DegP forms a spherical shell with 432 symmetry. In the crystal structure of DegP24, eight trimers are located at the vertices of an octahedron that assembles a protein shell of about 31 A thickness enclosing a large internal cavity about 110 A in diameter
vapor diffusion method
structure determination and analysis of the 24meric enzyme with complexed substrate beta-casein, cryo-electron microscopy images and three-dimensional structures, overview
structure of the hexameric HhoA in complex with the copurified peptide reveals the presence of three methionines in close proximity to the peptide-binding site of the PDZ domain. A zinc ion is accommodated within the central channel formed by a HhoA trimer. Neither calcium nor magnesium show affinity for HhoA
hanging drop vapor diffusion method
-
protease domain
-