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==Structure of Bacillus subtilis Nitric Oxide Synthase in complex with 6,6'-(2,2'-(5-amino-1,3-phenylene)bis(ethane-2,1-diyl))bis(4- methylpyridin-2-amine)== | ==Structure of Bacillus subtilis Nitric Oxide Synthase in complex with 6,6'-(2,2'-(5-amino-1,3-phenylene)bis(ethane-2,1-diyl))bis(4- methylpyridin-2-amine)== | ||
<StructureSection load='4d3j' size='340' side='right' caption='[[4d3j]], [[Resolution|resolution]] 1.67Å' scene=''> | <StructureSection load='4d3j' size='340' side='right' caption='[[4d3j]], [[Resolution|resolution]] 1.67Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d3i|4d3i]], [[4d3k|4d3k]], [[4d3m|4d3m]], [[4d3n|4d3n]], [[4d3o|4d3o]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d3i|4d3i]], [[4d3k|4d3k]], [[4d3m|4d3m]], [[4d3n|4d3n]], [[4d3o|4d3o]]</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_(NAD(P)H-dependent) Nitric-oxide synthase (NAD(P)H-dependent)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.165 1.14.13.165] </span></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_(NAD(P)H-dependent) Nitric-oxide synthase (NAD(P)H-dependent)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.165 1.14.13.165] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d3j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d3j RCSB], [http://www.ebi.ac.uk/pdbsum/4d3j PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d3j OCA], [http://pdbe.org/4d3j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d3j RCSB], [http://www.ebi.ac.uk/pdbsum/4d3j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d3j ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4d3j" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 23:01, 11 August 2016
Structure of Bacillus subtilis Nitric Oxide Synthase in complex with 6,6'-(2,2'-(5-amino-1,3-phenylene)bis(ethane-2,1-diyl))bis(4- methylpyridin-2-amine)Structure of Bacillus subtilis Nitric Oxide Synthase in complex with 6,6'-(2,2'-(5-amino-1,3-phenylene)bis(ethane-2,1-diyl))bis(4- methylpyridin-2-amine)
Structural highlights
Function[NOSO_BACSU] Catalyzes the production of nitric oxide. Publication Abstract from PubMedInhibition of bacterial nitric oxide synthase (bNOS) has the potential to improve the efficacy of antimicrobials used to treat infections by Gram-positive pathogens Staphylococcus aureus and Bacillus anthracis. However, inhibitor specificity toward bNOS over the mammalian NOS (mNOS) isoforms remains a challenge because of the near identical NOS active sites. One key structural difference between the NOS isoforms is the amino acid composition of the pterin cofactor binding site that is adjacent to the NOS active site. Previously, we demonstrated that a NOS inhibitor targeting both the active and pterin sites was potent and functioned as an antimicrobial ( Holden , , Proc. Natl. Acad. Sci. U.S.A. 2013 , 110 , 18127 ). Here we present additional crystal structures, binding analyses, and bacterial killing studies of inhibitors that target both the active and pterin sites of a bNOS and function as antimicrobials. Together, these data provide a framework for continued development of bNOS inhibitors, as each molecule represents an excellent chemical scaffold for the design of isoform selective bNOS inhibitors. Structure-Based Design of Bacterial Nitric Oxide Synthase Inhibitors.,Holden JK, Kang S, Hollingsworth SA, Li H, Lim N, Chen S, Huang H, Xue F, Tang W, Silverman RB, Poulos TL J Med Chem. 2015 Jan 6. PMID:25522110[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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