1ed6

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(New page: 200px<br /><applet load="1ed6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ed6, resolution 2.05&Aring;" /> '''BOVINE ENDOTHELIAL N...)
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[[Image:1ed6.gif|left|200px]]<br /><applet load="1ed6" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ed6.gif|left|200px]]<br /><applet load="1ed6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ed6, resolution 2.05&Aring;" />
caption="1ed6, resolution 2.05&Aring;" />
'''BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-NIO (H4B FREE)'''<br />
'''BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-NIO (H4B FREE)'''<br />
==Overview==
==Overview==
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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.
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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==
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1ED6 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 ACT, ZN, HEM, ILO, CAD 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ED6 OCA].
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1ED6 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=ACT:'>ACT</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=ILO:'>ILO</scene>, <scene name='pdbligand=CAD:'>CAD</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=1ED6 OCA].
==Reference==
==Reference==
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[[Category: Li, H.]]
[[Category: Li, H.]]
[[Category: Martasek, P.]]
[[Category: Martasek, P.]]
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[[Category: Masters, B.S.S.]]
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[[Category: Masters, B S.S.]]
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[[Category: Poulos, T.L.]]
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[[Category: Poulos, T L.]]
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[[Category: Raman, C.S.]]
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[[Category: Raman, C S.]]
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[[Category: Southan, G.J.]]
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[[Category: Southan, G J.]]
[[Category: ACT]]
[[Category: ACT]]
[[Category: CAD]]
[[Category: CAD]]
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[[Category: nitric oxide synthase]]
[[Category: nitric oxide synthase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:54:38 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:29 2008''

Revision as of 10:26, 21 February 2008


1ed6, resolution 2.05Å

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BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-NIO (H4B FREE)

Overview

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

1ED6 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.

Reference

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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