1ons: Difference between revisions

Latest revision as of 08:02, 14 February 2024

Crystal structure of Escherichia coli heat shock protein YedU

Structural highlights

1ons is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Ligands:	ZN
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.

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:https://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:https://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:https://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:https://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:https://dx.doi.org/10.1111/j.1365-2958.2011.07736.x

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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:https://dx.doi.org/10.1074/jbc.M205800200

[3] 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

[4] 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

[5] 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:https://dx.doi.org/10.1074/jbc.M408296200

[6] 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:https://dx.doi.org/10.1111/j.1365-2958.2006.05207.x

[7] 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:https://dx.doi.org/10.1128/AEM.02429-06

[8] 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:https://dx.doi.org/10.1111/j.1365-2958.2011.07736.x

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@@ Line 1: / Line 1: @@
-[[Image:1ons.png|left|200px]]
-{{STRUCTURE_1ons|  PDB=1ons  |  SCENE=  }}
+==Crystal structure of Escherichia coli heat shock protein YedU==
+<StructureSection load='1ons' size='340' side='right'caption='[[1ons]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-===Crystal structure of Escherichia coli heat shock protein YedU===
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ons]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ONS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ONS FirstGlance]. <br>
-{{ABSTRACT_PUBMED_14500888}}
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-==About this Structure==
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ons FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ons OCA], [https://pdbe.org/1ons PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ons RCSB], [https://www.ebi.ac.uk/pdbsum/1ons PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ons ProSAT]</span></td></tr>
-[[1ons]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ONS OCA].
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HCHA_ECOLI 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.<ref>PMID:7848303</ref> <ref>PMID:12235139</ref> <ref>PMID:12565879</ref> <ref>PMID:14731284</ref> <ref>PMID:15550391</ref> <ref>PMID:16796689</ref> <ref>PMID:17158627</ref> <ref>PMID:21696459</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/on/1ons_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <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/main_output.php?pdb_ID=1ons ConSurf].
+<div style="clear:both"></div>
 ==See Also==
-*[[Heat Shock Proteins|Heat Shock Proteins]]
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:014500888</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Fox, R O.]]
+[[Category: Large Structures]]
-[[Category: Zhao, Y.]]
+[[Category: Fox RO]]
-[[Category: Chaperone]]
+[[Category: Zhao Y]]
-[[Category: Heat shock protein]]
-[[Category: Hsp31]]
-[[Category: Protease]]
-[[Category: Stress response]]
-[[Category: Yedu]]

1ons: Difference between revisions

Latest revision as of 08:02, 14 February 2024

Crystal structure of Escherichia coli heat shock protein YedU

Structural highlights

Function

Evolutionary Conservation

See Also

References

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