5XR2

SAV0551

Summary for 5XR2

• Entry DOI: 10.2210/pdb5xr2/pdb
• Descriptor: Protein/nucleic acid deglycase HchA, LACTIC ACID, ZINC ION, ... (4 entities in total)
• Functional Keywords: hsp31, chaperone, glyoxalase iii
• Biological source: Staphylococcus aureus (strain Mu50 / ATCC 700699)
• Cellular location: Cytoplasm : P64312
• Total number of polymer chains: 8
• Total formula weight: 266515.47

Authors

Kim, H.J.,Kwon, A.R.,Lee, B.J. (deposition date: 2017-06-07, release date: 2017-11-01, Last modification date: 2023-11-22)

Primary citation

Kim, H.J.,Lee, K.Y.,Kwon, A.R.,Lee, B.J.
Structural and functional studies of SAV0551 fromStaphylococcus aureusas a chaperone and glyoxalase III.
Biosci. Rep., 37:-, 2017

PubMed Abstract: The DJ-1/ThiJ/pI superfamily of proteins is highly conserved across all biological kingdoms showing divergent multifunctions, such as chaperone, catalase, protease, and kinase. The common theme of these functions is responding to and managing various cellular stresses. DJ-1/ThiJ/pI superfamily members are classified into three subfamilies according to their quaternary structure (DJ-1-, YhbO-, and Hsp-types). The Hsp-type subfamily includes Hsp31, a chaperone and glyoxalase III. SAV0551, an Hsp-type subfamily member from , is a hypothetical protein that is predicted as Hsp31. Thus, to reveal the function and reaction mechanism of SAV0551, the crystal structure of SAV0551 was determined. The overall folds in SAV0551 are similar to other members of the Hsp-type subfamily. We have shown that SAV0551 functions as a chaperone and that the surface structure is crucial for holding unfolded substrates. As many DJ-1/ThiJ/pI superfamily proteins have been characterized as glyoxalase III, our study also demonstrates SAV0551 as a glyoxalase III that is independent of any cofactors. The reaction mechanism was evaluated via a glyoxylate-bound structure that mimics the hemithioacetal reaction intermediate. We have confirmed that the components required for reaction are present in the structure, including a catalytic triad for a catalytic action, His as a base, and a water molecule for hydrolysis. Our functional studies based on the crystal structures of native and glyoxylate-bound SAV0551 will provide a better understanding of the reaction mechanism of a chaperone and glyoxalase III.

PubMed: 29046369
DOI: 10.1042/BSR20171106

Experimental method

X-RAY DIFFRACTION (2.6 Å)