|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4qyx' size='340' side='right'caption='[[4qyx]], [[Resolution|resolution]] 1.69Å' scene=''> | | <StructureSection load='4qyx' size='340' side='right'caption='[[4qyx]], [[Resolution|resolution]] 1.69Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qyx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1rw7 1rw7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QYX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qyx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1rw7 1rw7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QYX FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">D9719.36, HSP31, YDR533C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4qyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qyx OCA], [https://pdbe.org/4qyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qyx RCSB], [https://www.ebi.ac.uk/pdbsum/4qyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qyx ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qyx OCA], [http://pdbe.org/4qyx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qyx RCSB], [http://www.ebi.ac.uk/pdbsum/4qyx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qyx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HSP31_YEAST HSP31_YEAST]] Probable protease. May act as a chaperone. | + | [https://www.uniprot.org/uniprot/HSP31_YEAST HSP31_YEAST] Probable protease. May act as a chaperone. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 21: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Amour, S T]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Collins, J L]] | + | [[Category: Amour ST]] |
| - | [[Category: Petsko, G A]] | + | [[Category: Collins JL]] |
| - | [[Category: Ringe, D]] | + | [[Category: Petsko GA]] |
| - | [[Category: Wilson, M A]] | + | [[Category: Ringe D]] |
| - | [[Category: Alpha-beta sandwich]] | + | [[Category: Wilson MA]] |
| - | [[Category: Dj-1/thij/pfpi superfamily]]
| + | |
| - | [[Category: Glyoxalase iii]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
HSP31_YEAST Probable protease. May act as a chaperone.
Publication Abstract from PubMed
The yeast gene YDR533C encodes a protein belonging to the DJ-1/ThiJ/PfpI superfamily. This family includes the human protein DJ-1, which is mutated in autosomal recessive early-onset Parkinson's disease. The function of DJ-1 and its yeast homologue YDR533Cp is unknown. We report here the crystal structure of YDR533Cp at 1.8-A resolution. The structure indicates that the closest relative to YDR533Cp is the Escherichia coli heat shock protein Hsp31 (YedU), which has both chaperone and protease activity. As expected, the overall fold of the core domain of YDR533Cp is also similar to that of DJ-1 and the bacterial protease PfpI. YDR533Cp contains a possible catalytic triad analogous to that of Hsp31 and an additional domain that is present in Hsp31 but is not seen in DJ-1 and other members of the family. The cysteine in this triad (Cys-138) is oxidized in this crystal structure, similar to modifications seen in the corresponding cysteine in the crystal structure of DJ-1. YDR533Cp appears to be a dimer both in solution and the crystal, but this dimer is formed by a different interface than that found in Hsp31 or other members of the superfamily.
The 1.8-A resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: a member of the DJ-1/ThiJ/PfpI superfamily.,Wilson MA, St Amour CV, Collins JL, Ringe D, Petsko GA Proc Natl Acad Sci U S A. 2004 Feb 10;101(6):1531-6. Epub 2004 Jan 26. PMID:14745011[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wilson MA, St Amour CV, Collins JL, Ringe D, Petsko GA. The 1.8-A resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: a member of the DJ-1/ThiJ/PfpI superfamily. Proc Natl Acad Sci U S A. 2004 Feb 10;101(6):1531-6. Epub 2004 Jan 26. PMID:14745011 doi:10.1073/pnas.0308089100
|
