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1m7z

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[[Image:1m7z.gif|left|200px]]
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{{STRUCTURE_1m7z| PDB=1m7z | SCENE= }}
{{STRUCTURE_1m7z| PDB=1m7z | SCENE= }}
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'''Structure of Nitric Oxide Synthase Heme Protein from Bacillus Subtilis with N-Hydroxy-Arginine and Tetrahydrofolate Bound'''
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===Structure of Nitric Oxide Synthase Heme Protein from Bacillus Subtilis with N-Hydroxy-Arginine and Tetrahydrofolate Bound===
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==Overview==
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Eukaryotic nitric oxide synthases (NOSs) produce nitric oxide to mediate intercellular signaling and protect against pathogens. Recently, proteins homologous to mammalian NOS oxygenase domains have been found in prokaryotes and one from Bacillus subtilis (bsNOS) has been demonstrated to produce nitric oxide [Adak, S., Aulak, K. S., and Stuehr, D. J. (2002) J. Biol. Chem. 277, 16167-16171]. We present structures of bsNOS complexed with the active cofactor tetrahydrofolate and the substrate L-arginine (L-Arg) or the intermediate N(omega)-hydroxy-L-arginine (NHA) to 1.9 or 2.2 A resolution, respectively. The bsNOS structure is similar to those of the mammalian NOS oxygenase domains (mNOS(ox)) except for the absence of an N-terminal beta-hairpin hook and zinc-binding region that interact with pterin and stabilize the mNOS(ox) dimer. Changes in patterns of residue conservation between bacterial and mammalian NOSs correlate to different binding modes for pterin side chains. Residue conservation on a surface patch surrounding an exposed heme edge indicates a likely interaction site for reductase proteins in all NOSs. The heme pockets of bsNOS and mNOS(ox) recognize L-Arg and NHA similarly, although a change from Val to Ile beside the substrate guanidinium may explain the 10-20-fold slower dissociation of product NO from the bacterial enzyme. Overall, these structures suggest that bsNOS functions naturally to produce nitrogen oxides from L-Arg and NHA in a pterin-dependent manner, but that the regulation and purpose of NO production by NOS may be quite different in B. subtilis than in mammals.
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{{ABSTRACT_PUBMED_12220171}}
==About this Structure==
==About this Structure==
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[[Category: Pterin]]
[[Category: Pterin]]
[[Category: Tetrahydrofolate]]
[[Category: Tetrahydrofolate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:44:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:24:42 2008''

Revision as of 20:24, 2 July 2008

Image:1m7z.png

Template:STRUCTURE 1m7z

Structure of Nitric Oxide Synthase Heme Protein from Bacillus Subtilis with N-Hydroxy-Arginine and Tetrahydrofolate Bound

Template:ABSTRACT PUBMED 12220171

About this Structure

1M7Z is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Structure of a nitric oxide synthase heme protein from Bacillus subtilis., Pant K, Bilwes AM, Adak S, Stuehr DJ, Crane BR, Biochemistry. 2002 Sep 17;41(37):11071-9. PMID:12220171

Page seeded by OCA on Wed Jul 2 23:24:42 2008

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