2g6h

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[[Image:2g6h.gif|left|200px]]<br /><applet load="2g6h" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2g6h.gif|left|200px]]
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caption="2g6h, resolution 2.00&Aring;" />
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'''Structure of rat nNOS heme domain (BH4 bound) in the reduced form'''<br />
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{{Structure
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|PDB= 2g6h |SIZE=350|CAPTION= <scene name='initialview01'>2g6h</scene>, resolution 2.00&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene> and <scene name='pdbligand=ARG:ARGININE'>ARG</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39]
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|GENE= Nos1, Bnos ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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}}
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'''Structure of rat nNOS heme domain (BH4 bound) in the reduced form'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2G6H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=H4B:'>H4B</scene> and <scene name='pdbligand=ARG:'>ARG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G6H OCA].
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2G6H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G6H OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16804678 16804678]
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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]
[[Category: Nitric-oxide synthase]]
[[Category: Nitric-oxide synthase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: nitric oxide synthase]]
[[Category: nitric oxide synthase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:28:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:01:00 2008''

Revision as of 15:01, 20 March 2008

Image:2g6h.gif


PDB ID 2g6h

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: , , , and
Gene: Nos1, Bnos (Rattus norvegicus)
Activity: Nitric-oxide synthase, with EC number 1.14.13.39
Coordinates: save as pdb, mmCIF, xml



Structure of rat nNOS heme domain (BH4 bound) in the reduced form


Overview

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.

About this Structure

2G6H is a Single protein structure of sequence from Rattus norvegicus. 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

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