1mjt

<table><tr><td colspan='2'>[[1mjt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MJT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1MJT FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ITU:ETHYLISOTHIOUREA'>ITU</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitric-oxide_synthase_(NADPH_dependent) Nitric-oxide synthase (NADPH dependent)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1mjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mjt OCA], [http://pdbe.org/1mjt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mjt RCSB], [http://www.ebi.ac.uk/pdbsum/1mjt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mjt ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/NOSO_STAAU NOSO_STAAU]] Catalyzes the production of nitric oxide (By similarity).

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:12467576</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1mjt" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bird, L E]]

[[Category: Ren, J]]

[[Category: Stammers, D K]]

[[Category: Bacterial]]

[[Category: Mrsa]]

[[Category: No]]

[[Category: Oxidoreductase]]

[[Category: Sano]]

[[Category: Seitu]]

[[Category: Synthase]]