2g6k: Difference between revisions

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New page: left|200px<br /><applet load="2g6k" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g6k, resolution 2.00Å" /> '''Structure of rat nNO...
 
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[[Image:2g6k.gif|left|200px]]<br /><applet load="2g6k" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2g6k.gif|left|200px]]<br /><applet load="2g6k" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2g6k, resolution 2.00&Aring;" />
caption="2g6k, resolution 2.00&Aring;" />
'''Structure of rat nNOS heme domain (BH4 bound) complexed with NO'''<br />
'''Structure of rat nNOS heme domain (BH4 bound) complexed with NO'''<br />


==Overview==
==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.
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==
2G6K 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, ARG and NO 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2G6K OCA].  
2G6K 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>, <scene name='pdbligand=ARG:'>ARG</scene> and <scene name='pdbligand=NO:'>NO</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=2G6K OCA].  


==Reference==
==Reference==
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[[Category: Jamal, J.]]
[[Category: Jamal, J.]]
[[Category: Li, H.]]
[[Category: Li, H.]]
[[Category: Poulos, T.L.]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:59:54 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:28:38 2008''