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New page: left|200px<br /><applet load="1mjt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mjt, resolution 2.40Å" /> '''CRYSTAL STRUCTURE OF...
 
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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;" />
caption="1mjt, resolution 2.40&Aring;" />
'''CRYSTAL STRUCTURE OF SANOS, A BACTERIAL NITRIC OXIDE SYNTHASE OXYGENASE PROTEIN, IN COMPLEX WITH NAD+ AND SEITU'''<br />
'''CRYSTAL STRUCTURE OF SANOS, A BACTERIAL NITRIC OXIDE SYNTHASE OXYGENASE PROTEIN, IN COMPLEX WITH NAD+ AND SEITU'''<br />


==Overview==
==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==
==About this Structure==
1MJT 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].  
1MJT 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==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Bird, L.E.]]
[[Category: Bird, L E.]]
[[Category: Ren, J.]]
[[Category: Ren, J.]]
[[Category: Stammers, D.K.]]
[[Category: Stammers, D K.]]
[[Category: HEM]]
[[Category: HEM]]
[[Category: ITU]]
[[Category: ITU]]
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[[Category: synthase]]
[[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''