1qjd

From Proteopedia

(Difference between revisions)

Current revision

Flavocytochrome C3 from Shewanella frigidimarina

Structural highlights

1qjd is a 1 chain structure with sequence from Shewanella frigidimarina. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FCCA_SHEFN Flavocytochrome that catalyzes the reduction of fumarate to succinate (PubMed:8093012). Is essential for fumarate respiration during anaerobic growth, acting as the terminal reductase (PubMed:9579067). Receives electrons from the membrane-bound tetraheme c-type cytochrome CymA (By similarity). Is essentially unidirectional, catalyzing only fumarate reduction (PubMed:8093012). Cannot reduce nitrite, dimethylsulphoxide, trimethylamine-N-oxide (TMAO) or sulfite (PubMed:8093012). In vitro, can use the artificial electron donor methyl viologen (PubMed:8093012).[UniProtKB:P83223]^[1] ^[2]

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 1.8 A resolution crystal structure of the tetraheme flavocytochrome c3, Fcc3, provides the first mechanistic insight into respiratory fumarate reductases or succinate dehydrogenases. The multi-redox center, three-domain protein shows a 40 A long 'molecular wire' allowing rapid conduction of electrons through a new type of cytochrome domain onto the active site flavin, driving the reduction of fumarate to succinate. In this structure a malate-like molecule is trapped in the enzyme active site. The interactions between this molecule and the enzyme suggest a clear mechanism for fumarate reduction in which the substrate is polarized and twisted, facilitating hydride transfer from the reduced flavin and subsequent proton transfer. The enzyme active site in the oxidized form is completely buried at the interface between the flavin-binding and the clamp domains. Movement of the cytochrome and clamp domains is postulated to allow release of the product.

Structural and mechanistic mapping of a unique fumarate reductase.,Taylor P, Pealing SL, Reid GA, Chapman SK, Walkinshaw MD Nat Struct Biol. 1999 Dec;6(12):1108-12. PMID:10581550^[3]

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

References

↑ Morris CJ, Black AC, Pealing SL, Manson FD, Chapman SK, Reid GA, Gibson DM, Ward FB. Purification and properties of a novel cytochrome: flavocytochrome c from Shewanella putrefaciens. Biochem J. 1994 Sep 1;302 ( Pt 2)(Pt 2):587-93. PMID:8093012 doi:10.1042/bj3020587
↑ Gordon EHJ, Pealing SL, Chapman SK, Ward FB, Reid GA. Physiological function and regulation of flavocytochrome c3, the soluble fumarate reductase from Shewanella putrefaciens NCIMB 400. Microbiology (Reading). 1998 Apr;144 ( Pt 4):937-945. PMID:9579067 doi:10.1099/00221287-144-4-937
↑ Taylor P, Pealing SL, Reid GA, Chapman SK, Walkinshaw MD. Structural and mechanistic mapping of a unique fumarate reductase. Nat Struct Biol. 1999 Dec;6(12):1108-12. PMID:10581550 doi:10.1038/70045

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1qjd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_frigidimarina Shewanella frigidimarina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QJD FirstGlance]. <br>
-</td></tr><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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TEO:MALATE+LIKE+INTERMEDIATE'>TEO</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]] 1.8&#8491;</td></tr>
+<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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TEO:MALATE+LIKE+INTERMEDIATE'>TEO</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=1qjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qjd OCA], [https://pdbe.org/1qjd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qjd RCSB], [https://www.ebi.ac.uk/pdbsum/1qjd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qjd ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/FCCA_SHEFN FCCA_SHEFN] Flavocytochrome that catalyzes the reduction of fumarate to succinate (PubMed:8093012). Is essential for fumarate respiration during anaerobic growth, acting as the terminal reductase (PubMed:9579067). Receives electrons from the membrane-bound tetraheme c-type cytochrome CymA (By similarity). Is essentially unidirectional, catalyzing only fumarate reduction (PubMed:8093012). Cannot reduce nitrite, dimethylsulphoxide, trimethylamine-N-oxide (TMAO) or sulfite (PubMed:8093012). In vitro, can use the artificial electron donor methyl viologen (PubMed:8093012).[UniProtKB:P83223]<ref>PMID:8093012</ref> <ref>PMID:9579067</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 12: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qj/1qjd_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 35: / Line 38: @@
 [[Category: Large Structures]]
 [[Category: Shewanella frigidimarina]]
-[[Category: Chapman, S K]]
+[[Category: Chapman SK]]
-[[Category: Pealing, S L]]
+[[Category: Pealing SL]]
-[[Category: Reid, G A]]
+[[Category: Reid GA]]
-[[Category: Taylor, P]]
+[[Category: Taylor P]]
-[[Category: Walkinshaw, M D]]
+[[Category: Walkinshaw MD]]
-[[Category: Fumarate reductase]]
-[[Category: Oxidoreductase]]
-[[Category: Respiratory fumarate reductase]]

1qjd

From Proteopedia

Current revision

Flavocytochrome C3 from Shewanella frigidimarina

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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