4d7h: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4d7h]] 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=4D7H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D7H FirstGlance]. <br> | <table><tr><td colspan='2'>[[4d7h]] 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=4D7H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D7H FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=M46:7-[2-[3-(3-FLUOROPHENYL)PROPYLAMINO]ETHYL]QUINOLIN-2-AMINE'>M46</scene>, <scene name='pdbligand=POL:N-PROPANOL'>POL</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.02Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=M46:7-[2-[3-(3-FLUOROPHENYL)PROPYLAMINO]ETHYL]QUINOLIN-2-AMINE'>M46</scene>, <scene name='pdbligand=POL:N-PROPANOL'>POL</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=4d7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d7h OCA], [https://pdbe.org/4d7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d7h RCSB], [https://www.ebi.ac.uk/pdbsum/4d7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d7h ProSAT]</span></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=4d7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d7h OCA], [https://pdbe.org/4d7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d7h RCSB], [https://www.ebi.ac.uk/pdbsum/4d7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d7h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/NOSO_BACSU NOSO_BACSU] Catalyzes the production of nitric oxide. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Latest revision as of 15:22, 20 December 2023
Structure of Bacillus subtilis nitric oxide synthase in complex with 7-(2-(3-(3-Fluorophenyl(propylamino)ethyl))quinolin-2- amineStructure of Bacillus subtilis nitric oxide synthase in complex with 7-(2-(3-(3-Fluorophenyl(propylamino)ethyl))quinolin-2- amine
Structural highlights
FunctionNOSO_BACSU Catalyzes the production of nitric oxide. Publication Abstract from PubMedBacterial infections associated with methicillin-resistant Staphylococcus aureus (MRSA) are a major economic burden to hospitals, and confer high rates of morbidity and mortality among those infected. Exploitation of novel therapeutic targets is thus necessary to combat this dangerous pathogen. Here, we report on the identification and characterization, including crystal structures, of two nitric oxide synthase (NOS) inhibitors that function as antimicrobials against MRSA. These data provide the first evidence that bacterial NOS (bNOS) inhibitors can work synergistically with oxidative stress to enhance MRSA killing. Crystal structures show that each inhibitor contacts an active site Ile residue in bNOS that is Val in the mammalian NOS isoforms. Mutagenesis studies show that the additional nonpolar contacts provided by the Ile in bNOS contribute to tighter binding toward the bacterial enzyme. Nitric Oxide Synthase as a Target for Methicillin-Resistant Staphylococcus aureus.,Holden JK, Kang S, Beasley FC, Cinelli MA, Li H, Roy SG, Dejam D, Edinger AL, Nizet V, Silverman RB, Poulos TL Chem Biol. 2015 Jun 18;22(6):785-92. doi: 10.1016/j.chembiol.2015.05.013. PMID:26091171[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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