1qjd: Difference between revisions
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< | ==Flavocytochrome C3 from Shewanella frigidimarina== | ||
<StructureSection load='1qjd' size='340' side='right'caption='[[1qjd]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
or the | <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</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]] | |||
Check<jmol> | |||
<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/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=1qjd ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:10581550</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1qjd" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Flavocytochrome 3D structures|Flavocytochrome 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: Shewanella frigidimarina]] | [[Category: Shewanella frigidimarina]] | ||
[[Category: Chapman | [[Category: Chapman SK]] | ||
[[Category: Pealing | [[Category: Pealing SL]] | ||
[[Category: Reid | [[Category: Reid GA]] | ||
[[Category: Taylor | [[Category: Taylor P]] | ||
[[Category: Walkinshaw | [[Category: Walkinshaw MD]] | ||
Latest revision as of 03:24, 21 November 2024
Flavocytochrome C3 from Shewanella frigidimarinaFlavocytochrome C3 from Shewanella frigidimarina
Structural highlights
FunctionFCCA_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 PubMedThe 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. See AlsoReferences
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