1e5d
From Proteopedia
(Difference between revisions)
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<StructureSection load='1e5d' size='340' side='right'caption='[[1e5d]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1e5d' size='340' side='right'caption='[[1e5d]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1e5d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1e5d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Megalodesulfovibrio_gigas Megalodesulfovibrio gigas]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E5D FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=1e5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e5d OCA], [https://pdbe.org/1e5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e5d RCSB], [https://www.ebi.ac.uk/pdbsum/1e5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e5d 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=1e5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e5d OCA], [https://pdbe.org/1e5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e5d RCSB], [https://www.ebi.ac.uk/pdbsum/1e5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e5d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ROO_MEGG1 ROO_MEGG1] Catalyzes the four-electron reduction of one oxygen molecule to two water molecules. | ||
== 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=1e5d 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=1e5d ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Desulfovibrio gigas is a strict anaerobe that contains a well-characterized metabolic pathway that enables it to survive transient contacts with oxygen. The terminal enzyme in this pathway, rubredoxin:oxygen oxidoreductase (ROO) reduces oxygen to water in a direct and safe way. The 2.5 A resolution crystal structure of ROO shows that each monomer of this homodimeric enzyme consists of a novel combination of two domains, a flavodoxin-like domain and a Zn-beta-lactamase-like domain that contains a di-iron center for dioxygen reduction. This is the first structure of a member of a superfamily of enzymes widespread in strict and facultative anaerobes, indicating its broad physiological significance. | ||
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| - | Structure of a dioxygen reduction enzyme from Desulfovibrio gigas.,Frazao C, Silva G, Gomes CM, Matias P, Coelho R, Sieker L, Macedo S, Liu MY, Oliveira S, Teixeira M, Xavier AV, Rodrigues-Pousada C, Carrondo MA, Le Gall J Nat Struct Biol. 2000 Nov;7(11):1041-5. PMID:11062560<ref>PMID:11062560</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1e5d" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Desulfovibrio gigas]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Carrondo | + | [[Category: Megalodesulfovibrio gigas]] |
| - | [[Category: Coelho | + | [[Category: Carrondo MA]] |
| - | [[Category: Frazao | + | [[Category: Coelho R]] |
| - | [[Category: | + | [[Category: Frazao C]] |
| - | [[Category: | + | [[Category: Gomes CM]] |
| - | [[Category: Liu | + | [[Category: Le Gall J]] |
| - | [[Category: Macedo | + | [[Category: Liu MY]] |
| - | [[Category: Matias | + | [[Category: Macedo S]] |
| - | [[Category: Oliveira | + | [[Category: Matias P]] |
| - | [[Category: Rodrigues-Pousada | + | [[Category: Oliveira S]] |
| - | [[Category: Sieker | + | [[Category: Rodrigues-Pousada C]] |
| - | [[Category: Silva | + | [[Category: Sieker L]] |
| - | [[Category: Teixeira | + | [[Category: Silva G]] |
| - | [[Category: Xavier | + | [[Category: Teixeira M]] |
| - | + | [[Category: Xavier AV]] | |
| - | + | ||
| - | + | ||
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Revision as of 09:58, 20 March 2024
RUBREDOXIN OXYGEN:OXIDOREDUCTASE (ROO) FROM ANAEROBE DESULFOVIBRIO GIGAS
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Categories: Large Structures | Megalodesulfovibrio gigas | Carrondo MA | Coelho R | Frazao C | Gomes CM | Le Gall J | Liu MY | Macedo S | Matias P | Oliveira S | Rodrigues-Pousada C | Sieker L | Silva G | Teixeira M | Xavier AV
