View source for 4ugk


==Structure of Bacillus subtilis Nitric Oxide Synthase in complex with 6-(2-(5-(2-(Dimethylamino)ethyl)pyridin-3-yl)ethyl)-4-methylpyridin-2- amine==
<StructureSection load='4ugk' size='340' side='right'caption='[[4ugk]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ugk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UGK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.62&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7S9:6-[2-[5-[2-(DIMETHYLAMINO)ETHYL]PYRIDIN-3-YL]ETHYL]-4-METHYL-PYRIDIN-2-AMINE'>7S9</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ugk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ugk OCA], [https://pdbe.org/4ugk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ugk RCSB], [https://www.ebi.ac.uk/pdbsum/4ugk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ugk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NOSO_BACSU NOSO_BACSU] Catalyzes the production of nitric oxide.
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== Publication Abstract from PubMed ==
Nitric oxide generated by bacterial nitric oxide synthase (NOS) increases the susceptibility of Gram-positive pathogens Staphylococcus aureus and Bacillus anthracis to oxidative stress, including antibiotic-induced oxidative stress. Not surprisingly, NOS inhibitors also improve the effectiveness of antimicrobials. Development of potent and selective bacterial NOS inhibitors is complicated by the high active site sequence and structural conservation shared with the mammalian NOS isoforms. To exploit bacterial NOS for the development of new therapeutics, recognition of alternative NOS surfaces and pharmacophores suitable for drug binding is required. Here, we report on a wide number of inhibitor-bound bacterial NOS crystal structures to identify several compounds that interact with surfaces unique to the bacterial NOS. Although binding studies indicate that these inhibitors weakly interact with the NOS active site, many of the inhibitors reported here provide a revised structural framework for the development of new antimicrobials that target bacterial NOS. In addition, mutagenesis studies reveal several key residues that unlock access to bacterial NOS surfaces that could provide the selectivity required to develop potent bacterial NOS inhibitors.

Inhibitor Bound Crystal Structures of Bacterial Nitric Oxide Synthase.,Holden JK, Dejam D, Lewis MC, Huang H, Kang S, Jing Q, Xue F, Silverman RB, Poulos TL Biochemistry. 2015 Jun 23. PMID:26062720<ref>PMID:26062720</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 4ugk" style="background-color:#fffaf0;"></div>

==See Also==
*[[Nitric Oxide Synthase 3D structures|Nitric Oxide Synthase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Large Structures]]
[[Category: Holden JK]]
[[Category: Poulos TL]]