1fol: Difference between revisions
New page: left|200px<br /><applet load="1fol" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fol, resolution 2.20Å" /> '''REDUCED BOVINE ENDOT... |
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[[Image:1fol.gif|left|200px]]<br /><applet load="1fol" size=" | [[Image:1fol.gif|left|200px]]<br /><applet load="1fol" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1fol, resolution 2.20Å" /> | caption="1fol, resolution 2.20Å" /> | ||
'''REDUCED BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-ARG(H4B-FREE)'''<br /> | '''REDUCED BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-ARG(H4B-FREE)'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of the endothelial nitric oxide synthase (NOS) heme | The crystal structure of the endothelial nitric oxide synthase (NOS) heme domain complexed with NO reveals close hydrogen bonding interactions between NO and the terminal guanidino nitrogen of the substrate, L-arginine. Dioxygen is expected to bind in a similar mode which will facilitate proton abstraction from L-Arg to dioxygen, a required step for O-O bond cleavage. Structures of mechanism-based NOS inhibitors, N(5)-(1-iminoethyl)-L-ornithine and N-(3-(aminomethyl)benzyl)acetamidine, provide clues on how this class of compounds operate as suicide substrate inhibitors leading to heme oxidation. | ||
==About this Structure== | ==About this Structure== | ||
1FOL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CAC, ACT, ZN, HEM, ARG and GOL 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:// | 1FOL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CAC:'>CAC</scene>, <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=ARG:'>ARG</scene> and <scene name='pdbligand=GOL:'>GOL</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=1FOL OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Li, H.]] | [[Category: Li, H.]] | ||
[[Category: Martasek, P.]] | [[Category: Martasek, P.]] | ||
[[Category: Masters, B | [[Category: Masters, B S.]] | ||
[[Category: Poulos, T | [[Category: Poulos, T L.]] | ||
[[Category: Raman, C | [[Category: Raman, C S.]] | ||
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: ARG]] | [[Category: ARG]] | ||
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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 12:40:57 2008'' |
Revision as of 13:40, 21 February 2008
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REDUCED BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-ARG(H4B-FREE)
OverviewOverview
The crystal structure of the endothelial nitric oxide synthase (NOS) heme domain complexed with NO reveals close hydrogen bonding interactions between NO and the terminal guanidino nitrogen of the substrate, L-arginine. Dioxygen is expected to bind in a similar mode which will facilitate proton abstraction from L-Arg to dioxygen, a required step for O-O bond cleavage. Structures of mechanism-based NOS inhibitors, N(5)-(1-iminoethyl)-L-ornithine and N-(3-(aminomethyl)benzyl)acetamidine, provide clues on how this class of compounds operate as suicide substrate inhibitors leading to heme oxidation.
About this StructureAbout this Structure
1FOL is a Single protein structure of sequence from Bos taurus with , , , , and as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 Full crystallographic information is available from OCA.
ReferenceReference
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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