1mjt: Difference between revisions

Revision as of 14:55, 21 February 2008

CRYSTAL STRUCTURE OF SANOS, A BACTERIAL NITRIC OXIDE SYNTHASE OXYGENASE PROTEIN, IN COMPLEX WITH NAD+ AND SEITU

OverviewOverview

Prokaryotic genes related to the oxygenase domain of mammalian nitric oxide synthases (NOSs) have recently been identified. Although they catalyze the same reaction as the eukaryotic NOS oxygenase domain, their biological function(s) are unknown. In order to explore rationally the biochemistry and evolution of the prokaryotic NOS family, we have determined the crystal structure of SANOS, from methicillin-resistant Staphylococcus aureus (MRSA), to 2.4 A. Haem and S-ethylisothiourea (SEITU) are bound at the SANOS active site, while the intersubunit site, occupied by the redox cofactor tetrahydrobiopterin (H(4)B) in mammalian NOSs, has NAD(+) bound in SANOS. In common with all bacterial NOSs, SANOS lacks the N-terminal extension responsible for stable dimerization in mammalian isoforms, but has alternative interactions to promote dimer formation.

About this StructureAbout this Structure

1MJT is a Single protein structure of sequence from Staphylococcus aureus with , , and as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of SANOS, a bacterial nitric oxide synthase oxygenase protein from Staphylococcus aureus., Bird LE, Ren J, Zhang J, Foxwell N, Hawkins AR, Charles IG, Stammers DK, Structure. 2002 Dec;10(12):1687-96. PMID:12467576

Page seeded by OCA on Thu Feb 21 13:55:55 2008

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OCA

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-[[Image:1mjt.gif|left|200px]]<br /><applet load="1mjt" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1mjt.gif|left|200px]]<br /><applet load="1mjt" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1mjt, resolution 2.40&Aring;" />
 '''CRYSTAL STRUCTURE OF SANOS, A BACTERIAL NITRIC OXIDE SYNTHASE OXYGENASE PROTEIN, IN COMPLEX WITH NAD+ AND SEITU'''<br />
 ==Overview==
-Prokaryotic genes related to the oxygenase domain of mammalian nitric, oxide synthases (NOSs) have recently been identified. Although they, catalyze the same reaction as the eukaryotic NOS oxygenase domain, their, biological function(s) are unknown. In order to explore rationally the, biochemistry and evolution of the prokaryotic NOS family, we have, determined the crystal structure of SANOS, from methicillin-resistant, Staphylococcus aureus (MRSA), to 2.4 A. Haem and S-ethylisothiourea, (SEITU) are bound at the SANOS active site, while the intersubunit site, occupied by the redox cofactor tetrahydrobiopterin (H(4)B) in mammalian, NOSs, has NAD(+) bound in SANOS. In common with all bacterial NOSs, SANOS, lacks the N-terminal extension responsible for stable dimerization in, mammalian isoforms, but has alternative interactions to promote dimer, formation.
+Prokaryotic genes related to the oxygenase domain of mammalian nitric oxide synthases (NOSs) have recently been identified. Although they catalyze the same reaction as the eukaryotic NOS oxygenase domain, their biological function(s) are unknown. In order to explore rationally the biochemistry and evolution of the prokaryotic NOS family, we have determined the crystal structure of SANOS, from methicillin-resistant Staphylococcus aureus (MRSA), to 2.4 A. Haem and S-ethylisothiourea (SEITU) are bound at the SANOS active site, while the intersubunit site, occupied by the redox cofactor tetrahydrobiopterin (H(4)B) in mammalian NOSs, has NAD(+) bound in SANOS. In common with all bacterial NOSs, SANOS lacks the N-terminal extension responsible for stable dimerization in mammalian isoforms, but has alternative interactions to promote dimer formation.
 ==About this Structure==
-MJT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with SUC, HEM, ITU and NAD 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=1MJT OCA].
+MJT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=SUC:'>SUC</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=ITU:'>ITU</scene> and <scene name='pdbligand=NAD:'>NAD</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=1MJT OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Staphylococcus aureus]]
-[[Category: Bird, L.E.]]
+[[Category: Bird, L E.]]
 [[Category: Ren, J.]]
-[[Category: Stammers, D.K.]]
+[[Category: Stammers, D K.]]
 [[Category: HEM]]
 [[Category: ITU]]
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 [[Category: synthase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:27:56 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:55 2008''