1d4e: Difference between revisions

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==CRYSTAL STRUCTURE OF THE FLAVOCYTOCHROME C FUMARATE REDUCTASE OF SHEWANELLA PUTREFACIENS STRAIN MR-1 COMPLEXED WITH FUMARATE==
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<StructureSection load='1d4e' size='340' side='right'caption='[[1d4e]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1d4e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_oneidensis Shewanella oneidensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D4E FirstGlance]. <br>
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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]] 2.8&#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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
{{STRUCTURE_1d4e|  PDB=1d4e  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d4e OCA], [https://pdbe.org/1d4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d4e RCSB], [https://www.ebi.ac.uk/pdbsum/1d4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d4e ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/FCCA_SHEON FCCA_SHEON] Flavocytochrome that catalyzes the reduction of fumarate to succinate (PubMed:12196158, PubMed:12899636, PubMed:22458729). Is essential for fumarate respiration during anaerobic growth, acting as the terminal reductase (By similarity). Receives electrons from the membrane-bound tetraheme c-type cytochrome CymA (PubMed:12196158, PubMed:12899636, PubMed:19837833, PubMed:22458729). Under ferric iron-reducing conditions, can be part of an electron transport chain to ferric iron, by accepting electrons from CymA and transfering them to the c-type cytochrome MtrA (PubMed:19837833). Also plays an important role in the reduction of selenite to elemental selenium (PubMed:24435070). May act as a transient electron storage protein (PubMed:19837833).[UniProtKB:Q07WU7]<ref>PMID:12196158</ref> <ref>PMID:12899636</ref> <ref>PMID:19837833</ref> <ref>PMID:22458729</ref> <ref>PMID:24435070</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
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    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1d4e ConSurf].
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== Publication Abstract from PubMed ==
Fumarate respiration is one of the most widespread types of anaerobic respiration. The soluble fumarate reductase of Shewanella putrefaciens MR-1 is a periplasmic tetraheme flavocytochrome c. The crystal structures of the enzyme were solved to 2.9 A for the uncomplexed form and to 2.8 A and 2.5 A for the fumarate and the succinate-bound protein, respectively. The structures reveal a flexible capping domain linked to the FAD-binding domain. A catalytic mechanism for fumarate reduction based on the structure of the complexed protein is proposed. The mechanism for the reverse reaction is a model for the homologous succinate dehydrogenase (complex II) of the respiratory chain. In flavocytochrome c fumarate reductase, all redox centers are in van der Waals contact with one another, thus providing an efficient conduit of electrons from the hemes via the FAD to fumarate.


===CRYSTAL STRUCTURE OF THE FLAVOCYTOCHROME C FUMARATE REDUCTASE OF SHEWANELLA PUTREFACIENS STRAIN MR-1 COMPLEXED WITH FUMARATE===
Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1.,Leys D, Tsapin AS, Nealson KH, Meyer TE, Cusanovich MA, Van Beeumen JJ Nat Struct Biol. 1999 Dec;6(12):1113-7. PMID:10581551<ref>PMID:10581551</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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(as it appears on PubMed at http://www.pubmed.gov), where 10581551 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_10581551}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1D4E is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Shewanella_putrefaciens Shewanella putrefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D4E OCA].
[[Category: Shewanella oneidensis]]
 
[[Category: Cusanovich MA]]
==Reference==
[[Category: Leys D]]
<ref group="xtra">PMID:10581551</ref><references group="xtra"/>
[[Category: Meyer TE]]
[[Category: Shewanella putrefaciens]]
[[Category: Tsapin AS]]
[[Category: Succinate dehydrogenase]]
[[Category: Van Beeumen JJ]]
[[Category: Beeumen, J J.Van.]]
[[Category: Cusanovich, M A.]]
[[Category: Leys, D.]]
[[Category: Meyer, T E.]]
[[Category: Tsapin, A S.]]
[[Category: Tetraheme flavocytochrome c fumarate reductase]]
 
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