1qo8: Difference between revisions
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[[Image:1qo8.gif|left|200px]] | [[Image:1qo8.gif|left|200px]] | ||
'''THE STRUCTURE OF THE OPEN CONFORMATION OF A FLAVOCYTOCHROME C3 FUMARATE REDUCTASE''' | {{Structure | ||
|PDB= 1qo8 |SIZE=350|CAPTION= <scene name='initialview01'>1qo8</scene>, resolution 2.15Å | |||
|SITE= <scene name='pdbsite=AC1:Hem+Binding+Site+For+Resdiue+A601'>AC1</scene>, <scene name='pdbsite=AC2:Hem+Binding+Site+For+Resdiue+A602'>AC2</scene>, <scene name='pdbsite=AC3:Hem+Binding+Site+For+Resdiue+A603'>AC3</scene>, <scene name='pdbsite=AC4:Hem+Binding+Site+For+Resdiue+A604'>AC4</scene>, <scene name='pdbsite=AC5:Fad+Binding+Site+For+Resdiue+A605'>AC5</scene>, <scene name='pdbsite=AC6:Hem+Binding+Site+For+Resdiue+D601'>AC6</scene>, <scene name='pdbsite=AC7:Hem+Binding+Site+For+Resdiue+D602'>AC7</scene>, <scene name='pdbsite=AC8:Hem+Binding+Site+For+Residue+D603'>AC8</scene>, <scene name='pdbsite=AC9:Hem+Binding+Site+For+Residue+D604'>AC9</scene> and <scene name='pdbsite=BC1:Fad+Binding+Site+For+Residue+D605'>BC1</scene> | |||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</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] | |||
|GENE= | |||
}} | |||
'''THE STRUCTURE OF THE OPEN CONFORMATION OF A FLAVOCYTOCHROME C3 FUMARATE REDUCTASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1QO8 is a [ | 1QO8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Shewanella_frigidimarina Shewanella frigidimarina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QO8 OCA]. | ||
==Reference== | ==Reference== | ||
Open conformation of a flavocytochrome c3 fumarate reductase., Bamford V, Dobbin PS, Richardson DJ, Hemmings AM, Nat Struct Biol. 1999 Dec;6(12):1104-7. PMID:[http:// | Open conformation of a flavocytochrome c3 fumarate reductase., Bamford V, Dobbin PS, Richardson DJ, Hemmings AM, Nat Struct Biol. 1999 Dec;6(12):1104-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10581549 10581549] | ||
[[Category: Shewanella frigidimarina]] | [[Category: Shewanella frigidimarina]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:40:23 2008'' | ||
Revision as of 11:40, 20 March 2008
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| 1qo8, resolution 2.15Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Sites: | AC1, AC2, AC3, AC4, AC5, AC6, AC7, AC8, AC9 and BC1 | ||||||||||||
| Ligands: | HEM and FAD | ||||||||||||
| Activity: | Succinate dehydrogenase, with EC number 1.3.99.1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
THE STRUCTURE OF THE OPEN CONFORMATION OF A FLAVOCYTOCHROME C3 FUMARATE REDUCTASE
Overview
Fumarate reductases and succinate dehydrogenases play central roles in the metabolism of eukaryotic and prokaryotic cells. A recent medium resolution structure of the Escherichia coli fumarate reductase (Frd) has revealed the overall organization of the membrane-bound complex. Here we present the first high resolution X-ray crystal structure of a water-soluble bacterial fumarate reductase in an open conformation. This structure reveals a mobile domain that modulates substrate access to the active site and provides new insights into the mechanism of this widespread and important family of FAD-containing respiratory proteins.
About this Structure
1QO8 is a Single protein structure of sequence from Shewanella frigidimarina. Full crystallographic information is available from OCA.
Reference
Open conformation of a flavocytochrome c3 fumarate reductase., Bamford V, Dobbin PS, Richardson DJ, Hemmings AM, Nat Struct Biol. 1999 Dec;6(12):1104-7. PMID:10581549
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