1d4d
From Proteopedia
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|PDB= 1d4d |SIZE=350|CAPTION= <scene name='initialview01'>1d4d</scene>, resolution 2.5Å | |PDB= 1d4d |SIZE=350|CAPTION= <scene name='initialview01'>1d4d</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1d4c|1D4C]], [[1d4d|1D4D]], [[1d4e|1D4E]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d4d OCA], [http://www.ebi.ac.uk/pdbsum/1d4d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d4d RCSB]</span> | ||
}} | }} | ||
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[[Category: Meyer, T E.]] | [[Category: Meyer, T E.]] | ||
[[Category: Tsapin, A S.]] | [[Category: Tsapin, A S.]] | ||
| - | [[Category: FAD]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: SIN]] | ||
[[Category: tetraheme flavocytochrome c fumarate reductase]] | [[Category: tetraheme flavocytochrome c fumarate reductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:34:41 2008'' |
Revision as of 16:34, 30 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Succinate dehydrogenase, with EC number 1.3.99.1 | ||||||
| Related: | 1D4C, 1D4D, 1D4E
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE SUCCINATE COMPLEXED FORM OF THE FLAVOCYTOCHROME C FUMARATE REDUCTASE OF SHEWANELLA PUTREFACIENS STRAIN MR-1
Overview
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.
About this Structure
1D4D is a Single protein structure of sequence from Shewanella putrefaciens. Full crystallographic information is available from OCA.
Reference
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
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