2g6o

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{{STRUCTURE_2g6o| PDB=2g6o | SCENE= }}
{{STRUCTURE_2g6o| PDB=2g6o | SCENE= }}
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'''Structure of bovine eNOS heme domain (BH4-free) complexed with CO'''
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===Structure of bovine eNOS heme domain (BH4-free) complexed with CO===
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==Overview==
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Crystal structures are reported for the endothelial nitric oxide synthase (eNOS)-arginine-CO ternary complex as well as the neuronal nitric oxide synthase (nNOS) heme domain complexed with L: -arginine and diatomic ligands, CO or NO, in the presence of the native cofactor, tetrahydrobiopterin, or its oxidized analogs, dihydrobiopterin and 4-aminobiopterin. The nature of the biopterin has no influence on the diatomic ligand binding. The binding geometries of diatomic ligands to nitric oxide synthase (NOS) follow the {MXY}(n) formalism developed from the inorganic diatomic-metal complexes. The structures reveal some subtle structural differences between eNOS and nNOS when CO is bound to the heme which correlate well with the differences in CO stretching frequencies observed by resonance Raman techniques. The detailed hydrogen-bonding geometries depicted in the active site of nNOS structures indicate that it is the ordered active-site water molecule rather than the substrate itself that would most likely serve as a direct proton donor to the diatomic ligands (CO, NO, as well as O(2)) bound to the heme. This has important implications for the oxygen activation mechanism critical to NOS catalysis.
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The line below this paragraph, {{ABSTRACT_PUBMED_16804678}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_16804678}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structural studies of constitutive nitric oxide synthases with diatomic ligands bound., Li H, Igarashi J, Jamal J, Yang W, Poulos TL, J Biol Inorg Chem. 2006 Sep;11(6):753-68. Epub 2006 Jun 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16804678 16804678]
Structural studies of constitutive nitric oxide synthases with diatomic ligands bound., Li H, Igarashi J, Jamal J, Yang W, Poulos TL, J Biol Inorg Chem. 2006 Sep;11(6):753-68. Epub 2006 Jun 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16804678 16804678]
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Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors., Li H, Raman CS, Martasek P, Masters BS, Poulos TL, Biochemistry. 2001 May 8;40(18):5399-406. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11331003 11331003]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Nitric-oxide synthase]]
[[Category: Nitric-oxide synthase]]
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[[Category: Heme protein]]
[[Category: Heme protein]]
[[Category: Nitric oxide synthase]]
[[Category: Nitric oxide synthase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:45:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:38:19 2008''

Revision as of 18:38, 27 July 2008

Image:2g6o.png

Template:STRUCTURE 2g6o

Structure of bovine eNOS heme domain (BH4-free) complexed with CO

Template:ABSTRACT PUBMED 16804678

About this Structure

2G6O is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Structural studies of constitutive nitric oxide synthases with diatomic ligands bound., Li H, Igarashi J, Jamal J, Yang W, Poulos TL, J Biol Inorg Chem. 2006 Sep;11(6):753-68. Epub 2006 Jun 28. PMID:16804678

Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors., Li H, Raman CS, Martasek P, Masters BS, Poulos TL, Biochemistry. 2001 May 8;40(18):5399-406. PMID:11331003

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