1dw2: Difference between revisions
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[[Image:1dw2.gif|left|200px]] | [[Image:1dw2.gif|left|200px]] | ||
'''STRUCTURE OF THE NITRIC OXIDE COMPLEX OF REDUCED SHP, AN OXYGEN BINDING CYTOCHROME C''' | {{Structure | ||
|PDB= 1dw2 |SIZE=350|CAPTION= <scene name='initialview01'>1dw2</scene>, resolution 2.2Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=NO:NITROGEN OXIDE'>NO</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF THE NITRIC OXIDE COMPLEX OF REDUCED SHP, AN OXYGEN BINDING CYTOCHROME C''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DW2 is a [ | 1DW2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DW2 OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structures of an oxygen-binding cytochrome c from Rhodobacter sphaeroides., Leys D, Backers K, Meyer TE, Hagen WR, Cusanovich MA, Van Beeumen JJ, J Biol Chem. 2000 May 26;275(21):16050-6. PMID:[http:// | Crystal structures of an oxygen-binding cytochrome c from Rhodobacter sphaeroides., Leys D, Backers K, Meyer TE, Hagen WR, Cusanovich MA, Van Beeumen JJ, J Biol Chem. 2000 May 26;275(21):16050-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10821858 10821858] | ||
[[Category: Rhodobacter sphaeroides]] | [[Category: Rhodobacter sphaeroides]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nitric oxide]] | [[Category: nitric oxide]] | ||
''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 10:45:21 2008'' | ||
Revision as of 11:45, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE NITRIC OXIDE COMPLEX OF REDUCED SHP, AN OXYGEN BINDING CYTOCHROME C
OverviewOverview
The photosynthetic bacterium Rhodobacter sphaeroides produces a heme protein (SHP), which is an unusual c-type cytochrome capable of transiently binding oxygen during autooxidation. Similar proteins have not only been observed in other photosynthetic bacteria but also in the obligate methylotroph Methylophilus methylotrophus and the metal reducing bacterium Shewanella putrefaciens. A three-dimensional structure of SHP was derived using the multiple isomorphous replacement phasing method. Besides a model for the oxidized state (to 1.82 A resolution), models for the reduced state (2.1 A resolution), the oxidized molecule liganded with cyanide (1. 90 A resolution), and the reduced molecule liganded with nitric oxide (2.20 A resolution) could be derived. The SHP structure represents a new variation of the class I cytochrome c fold. The oxidized state reveals a novel sixth heme ligand, Asn(88), which moves away from the iron upon reduction or when small molecules bind. The distal side of the heme has a striking resemblance to other heme proteins that bind gaseous compounds. In SHP the liberated amide group of Asn(88) stabilizes solvent-shielded ligands through a hydrogen bond.
About this StructureAbout this Structure
1DW2 is a Single protein structure of sequence from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of an oxygen-binding cytochrome c from Rhodobacter sphaeroides., Leys D, Backers K, Meyer TE, Hagen WR, Cusanovich MA, Van Beeumen JJ, J Biol Chem. 2000 May 26;275(21):16050-6. PMID:10821858
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