PDBsum entry 1qvv

Structural genomics, unknown function

PDB id: 1qvv

Contents

Protein chains

234 a.a. *

Waters ×325

* Residue conservation analysis

PDB id:

1qvv

Name:

Structural genomics, unknown function

Title:

Crystal structure of the s. Cerevisiae ydr533c protein

Structure:

Ydr533c protein. Chain: a, b, c, d. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: ydr533c. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.35Å R-factor: 0.228 R-free: 0.283

Authors:

M.Graille,N.Leulliot,S.Quevillon-Cheruel,H.Van Tilbeurgh

Key ref:

M.Graille et al. (2004). Crystal structure of the YDR533c S. cerevisiae protein, a class II member of the Hsp31 family. Structure, 12, 839-847. PubMed id: 15130476 DOI: 10.1016/j.str.2004.02.030

Date:

29-Aug-03 Release date: 30-Mar-04

Protein chains

Q04432  (HSP31_YEAST) -  Glutathione-independent glyoxalase HSP31 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 237 a.a.

Struc: 234 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.4.2.1.130 - D-lactate dehydratase.
• Reaction: methylglyoxal + H2O = (R)-lactate + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1016/j.str.2004.02.030

Structure 12:839-847 (2004)

PubMed id: 15130476

Crystal structure of the YDR533c S. cerevisiae protein, a class II member of the Hsp31 family.

M.Graille, S.Quevillon-Cheruel, N.Leulliot, C.Z.Zhou, I.L.de la Sierra Gallay, L.Jacquamet, J.L.Ferrer, D.Liger, A.Poupon, J.Janin, H.van Tilbeurgh.

ABSTRACT

The ORF YDR533c from Saccharomyces cerevisiae codes for a 25.5 kDa protein of unknown biochemical function. Transcriptome analysis of yeast has shown that this gene is activated in response to various stress conditions together with proteins belonging to the heat shock family. In order to clarify its biochemical function, we determined the crystal structure of YDR533c to 1.85 A resolution by the single anomalous diffraction method. The protein possesses an alpha/beta hydrolase fold and a putative Cys-His-Glu catalytic triad common to a large enzyme family containing proteases, amidotransferases, lipases, and esterases. The protein has strong structural resemblance with the E. coli Hsp31 protein and the intracellular protease I from Pyrococcus horikoshii, which are considered class I and class III members of the Hsp31 family, respectively. Detailed structural analysis strongly suggests that the YDR533c protein crystal structure is the first one of a class II member of the Hsp31 family.

Selected figure(s)

Figure 3.
Figure 3. The Putative Catalytic Triad(A) Hydrophobic surface representation of the YDR533c dimer. Polar and hydrophobic residues are colored in white and red, respectively. The cysteine 138 side chain is shown as sticks. The putative active site pocket from one monomer is highlighted by dotted lines.(B) Superimposition of the YDR533c (green), E. coli Hsp31 (yellow), and PhPI (blue) catalytic triads (the proper triad acidic residue corresponds to Glu170). The DJ-1 putative catalytic dyad is show in pink. Only the YD533c numbering is indicated.

The above figure is reprinted by permission from Cell Press: Structure (2004, 12, 839-847) copyright 2004.

Figure was selected by an automated process.