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| - | [[Image:1m7v.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1m7v| PDB=1m7v | SCENE= }} | | {{STRUCTURE_1m7v| PDB=1m7v | SCENE= }} |
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| - | '''STRUCTURE OF A NITRIC OXIDE SYNTHASE HEME PROTEIN FROM BACILLUS SUBTILIS WITH TETRAHYDROFOLATE AND ARGININE BOUND'''
| + | ===STRUCTURE OF A NITRIC OXIDE SYNTHASE HEME PROTEIN FROM BACILLUS SUBTILIS WITH TETRAHYDROFOLATE AND ARGININE 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12220171}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12220171 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12220171}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Nitric oxide]] | | [[Category: Nitric oxide]] |
| | [[Category: Pterin oxygenase]] | | [[Category: Pterin oxygenase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:44:41 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:24:21 2008'' |
Revision as of 20:24, 2 July 2008
Template:STRUCTURE 1m7v
STRUCTURE OF A NITRIC OXIDE SYNTHASE HEME PROTEIN FROM BACILLUS SUBTILIS WITH TETRAHYDROFOLATE AND ARGININE BOUND
Template:ABSTRACT PUBMED 12220171
About this Structure
1M7V 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 23:24:21 2008
