1a8l

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<StructureSection load='1a8l' size='340' side='right'caption='[[1a8l]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1a8l' size='340' side='right'caption='[[1a8l]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1a8l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A8L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A8L FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1a8l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A8L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A8L FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8l OCA], [https://pdbe.org/1a8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a8l RCSB], [https://www.ebi.ac.uk/pdbsum/1a8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8l ProSAT]</span></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=1a8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8l OCA], [https://pdbe.org/1a8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a8l RCSB], [https://www.ebi.ac.uk/pdbsum/1a8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8l ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q51760_9EURY Q51760_9EURY]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1a8l 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=1a8l ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Protein disulfide bond formation is a rate limiting step in protein folding and is catalyzed by enzymes belonging to the protein disulfide oxidoreductase superfamily, including protein disulfide isomerase (PDI) in eucarya and DsbA in bacteria. The first high resolution X-ray crystal structure of a protein disulfide oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus reveals structural details that suggest a relation to eukaryotic PDI. The protein consists of two homologous structural units with low sequence identity. Each unit contains a thioredoxin fold with a distinct CXXC active site motif. The accessibilities of both active sites are rather different as are, very likely, their redox properties. The protein shows the ability to catalyze the oxidation of dithiols as well as the reduction of disulfide bridges.
 
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A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units.,Ren B, Tibbelin G, de Pascale D, Rossi M, Bartolucci S, Ladenstein R Nat Struct Biol. 1998 Jul;5(7):602-11. PMID:9665175<ref>PMID:9665175</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1a8l" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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*[[Protein disulfide oxidoreductase|Protein disulfide oxidoreductase]]
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*[[Protein disulfide oxidoreductase 3D structures|Protein disulfide oxidoreductase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43587]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bartolucci, S]]
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[[Category: Pyrococcus furiosus]]
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[[Category: Ladenstein, R]]
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[[Category: Bartolucci S]]
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[[Category: Pascale, D]]
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[[Category: Ladenstein R]]
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[[Category: Ren, B]]
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[[Category: Pascale D]]
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[[Category: Rossi, M]]
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[[Category: Ren B]]
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[[Category: Tibbelin, G]]
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[[Category: Rossi M]]
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[[Category: Oxidoreductase]]
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[[Category: Tibbelin G]]
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[[Category: Pdi]]
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[[Category: Thioredoxin fold]]
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Revision as of 15:22, 13 March 2024

PROTEIN DISULFIDE OXIDOREDUCTASE FROM ARCHAEON PYROCOCCUS FURIOSUS

PDB ID 1a8l

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