1ons

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Revision as of 10:03, 1 November 2017

Crystal structure of Escherichia coli heat shock protein YedU

Structural highlights

1ons is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	HCHA OR B1967 ("Bacillus coli" Migula 1895)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HCHA_ECOLI] Functions as a holding molecular chaperone (holdase) which stabilizes unfolding intermediates and rapidly releases them in an active form once stress has abated. Plays an important role in protecting cells from severe heat shock and starvation, as well as in acid resistance of stationary-phase cells. It uses temperature-induced exposure of structured hydrophobic domains to capture and stabilizes early unfolding and denatured protein intermediates under severe thermal stress. Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. It can also use phenylglyoxal as substrate. Glyoxalase activity protects cells against dicarbonyl stress. Displays an aminopeptidase activity that is specific against peptide substrates with alanine or basic amino acids (lysine, arginine) at N-terminus.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The mRNA of Escherichia coli yedU gene is induced 31-fold upon heat shock. The 31-kD YedU protein, also calls Hsp31, is highly conserved in several human pathogens and has chaperone activity. We solved the crystal structure of YedU at 2.2 A resolution. YedU monomer has an alpha/beta/alpha sandwich domain and a small alpha/beta domain. YedU is a dimer in solution, and its crystal structure indicates that a significant amount of surface area is buried upon dimerization. There is an extended hydrophobic patch that crosses the dimer interface on the surface of the protein. This hydrophobic patch is likely the substrate-binding site responsible for the chaperone activity. The structure also reveals a potential protease-like catalytic triad composed of Cys184, His185, and Asp213, although no enzymatic activity could be identified. YedU coordinates a metal ion using His85, His122, and Glu90. This 2-His-1-carboxylate motif is present in carboxypeptidase A (a zinc enzyme), and a number of dioxygenases and hydroxylases that utilize iron as a cofactor, suggesting another potential function for YedU.

The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites.,Zhao Y, Liu D, Kaluarachchi WD, Bellamy HD, White MA, Fox RO Protein Sci. 2003 Oct;12(10):2303-11. PMID:14500888^[9]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Misra K, Banerjee AB, Ray S, Ray M. Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione. Biochem J. 1995 Feb 1;305 ( Pt 3):999-1003. PMID:7848303
↑ Sastry MS, Korotkov K, Brodsky Y, Baneyx F. Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperatures. J Biol Chem. 2002 Nov 29;277(48):46026-34. Epub 2002 Sep 15. PMID:12235139 doi:http://dx.doi.org/10.1074/jbc.M205800200
↑ Malki A, Kern R, Abdallah J, Richarme G. Characterization of the Escherichia coli YedU protein as a molecular chaperone. Biochem Biophys Res Commun. 2003 Feb 7;301(2):430-6. PMID:12565879
↑ Mujacic M, Bader MW, Baneyx F. Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions. Mol Microbiol. 2004 Feb;51(3):849-59. PMID:14731284
↑ Malki A, Caldas T, Abdallah J, Kern R, Eckey V, Kim SJ, Cha SS, Mori H, Richarme G. Peptidase activity of the Escherichia coli Hsp31 chaperone. J Biol Chem. 2005 Apr 15;280(15):14420-6. Epub 2004 Nov 18. PMID:15550391 doi:http://dx.doi.org/10.1074/jbc.M408296200
↑ Mujacic M, Baneyx F. Regulation of Escherichia coli hchA, a stress-inducible gene encoding molecular chaperone Hsp31. Mol Microbiol. 2006 Jun;60(6):1576-89. PMID:16796689 doi:http://dx.doi.org/10.1111/j.1365-2958.2006.05207.x
↑ Mujacic M, Baneyx F. Chaperone Hsp31 contributes to acid resistance in stationary-phase Escherichia coli. Appl Environ Microbiol. 2007 Feb;73(3):1014-8. Epub 2006 Dec 8. PMID:17158627 doi:http://dx.doi.org/10.1128/AEM.02429-06
↑ Subedi KP, Choi D, Kim I, Min B, Park C. Hsp31 of Escherichia coli K-12 is glyoxalase III. Mol Microbiol. 2011 Aug;81(4):926-36. doi: 10.1111/j.1365-2958.2011.07736.x. Epub, 2011 Jul 6. PMID:21696459 doi:http://dx.doi.org/10.1111/j.1365-2958.2011.07736.x
↑ Zhao Y, Liu D, Kaluarachchi WD, Bellamy HD, White MA, Fox RO. The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites. Protein Sci. 2003 Oct;12(10):2303-11. PMID:14500888

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ons"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Escherichia coli heat shock protein YedU==
 <StructureSection load='1ons' size='340' side='right' caption='[[1ons]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HCHA OR B1967 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1ons FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ons OCA], [http://pdbe.org/1ons PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ons RCSB], [http://www.ebi.ac.uk/pdbsum/1ons PDBsum]</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=1ons FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ons OCA], [http://pdbe.org/1ons PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ons RCSB], [http://www.ebi.ac.uk/pdbsum/1ons PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ons ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ons ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1ons" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Heat Shock Proteins|Heat Shock Proteins]]
 == References ==
 <references/>

1ons

From Proteopedia

Revision as of 10:03, 1 November 2017

Crystal structure of Escherichia coli heat shock protein YedU

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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