2g6h
From Proteopedia
(New page: 200px<br /><applet load="2g6h" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g6h, resolution 2.00Å" /> '''Structure of rat nNO...) |
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| - | [[Image:2g6h.gif|left|200px]]<br /><applet load="2g6h" size=" | + | [[Image:2g6h.gif|left|200px]]<br /><applet load="2g6h" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2g6h, resolution 2.00Å" /> | caption="2g6h, resolution 2.00Å" /> | ||
'''Structure of rat nNOS heme domain (BH4 bound) in the reduced form'''<br /> | '''Structure of rat nNOS heme domain (BH4 bound) in the reduced form'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Crystal structures are reported for the endothelial nitric oxide synthase | + | 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== | ==About this Structure== | ||
| - | 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 ACT, ZN, HEM, H4B and ARG 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: Jamal, J.]] | [[Category: Jamal, J.]] | ||
[[Category: Li, H.]] | [[Category: Li, H.]] | ||
| - | [[Category: Poulos, T | + | [[Category: Poulos, T L.]] |
[[Category: Yang, W.]] | [[Category: Yang, W.]] | ||
[[Category: ACT]] | [[Category: ACT]] | ||
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[[Category: nitric oxide synthase]] | [[Category: nitric oxide synthase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:28:37 2008'' |
Revision as of 15:28, 21 February 2008
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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 with , , , and as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 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
Page seeded by OCA on Thu Feb 21 17:28:37 2008
Categories: Nitric-oxide synthase | Rattus norvegicus | Single protein | Igarashi, J. | Jamal, J. | Li, H. | Poulos, T L. | Yang, W. | ACT | ARG | H4B | HEM | ZN | Diatomic ligand | Heme protein | Nitric oxide synthase
