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| [[Image:1qjd.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1qjd| PDB=1qjd | SCENE= }} | | {{STRUCTURE_1qjd| PDB=1qjd | SCENE= }} |
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| '''FLAVOCYTOCHROME C3 FROM SHEWANELLA FRIGIDIMARINA'''
| | ===FLAVOCYTOCHROME C3 FROM SHEWANELLA FRIGIDIMARINA=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_10581550}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10581550 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10581550}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Fumarate reductase]] | | [[Category: Fumarate reductase]] |
| [[Category: Respiratory fumarate reductase]] | | [[Category: Respiratory fumarate reductase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:20:43 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:40:23 2008'' |