5g6e: Difference between revisions
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<StructureSection load='5g6e' size='340' side='right'caption='[[5g6e]], [[Resolution|resolution]] 2.11Å' scene=''> | <StructureSection load='5g6e' size='340' side='right'caption='[[5g6e]], [[Resolution|resolution]] 2.11Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5g6e]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5g6e]] 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=5G6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G6E 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=XH8:7-(((3-(PYRIDIN-3-YL)PROPYL)AMINO)METHYL)QUINOLIN-2-'>XH8</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.111Å</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=XH8:7-(((3-(PYRIDIN-3-YL)PROPYL)AMINO)METHYL)QUINOLIN-2-'>XH8</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=5g6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g6e OCA], [https://pdbe.org/5g6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g6e RCSB], [https://www.ebi.ac.uk/pdbsum/5g6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g6e ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</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 == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus subtilis subsp. subtilis str. 168]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Holden | [[Category: Holden JK]] | ||
[[Category: Poulos | [[Category: Poulos TL]] | ||
Latest revision as of 16:40, 26 July 2023
Structure of Bacillus subtilis Nitric Oxide Synthase in complex with 7-(((3-(Pyridin-3-yl)propyl)amino)methyl)quinolin-2-amineStructure of Bacillus subtilis Nitric Oxide Synthase in complex with 7-(((3-(Pyridin-3-yl)propyl)amino)methyl)quinolin-2-amine
Structural highlights
FunctionNOSO_BACSU Catalyzes the production of nitric oxide. Publication Abstract from PubMedNitric oxide (NO) is produced in Gram-positive pathogens Bacillus anthracis and Staphylococcus aureus by the bacterial isoform of nitric oxide synthase (NOS). Inhibition of bacterial nitric oxide synthase (bNOS) has been identified as a promising antibacterial strategy for targeting methicillin-resistant Staphylocoocus aureus1. One class of NOS inhibitors that demonstrates antimicrobial efficacy utilizes an aminoquinoline scaffold. Here we report on a variety of aminoquinolines that target the bacterial NOS active site, in part, by binding to a hydrophobic patch that is unique to bNOS. Through mutagenesis and crystallographic studies, our findings demonstrate that aminoquinolines are an excellent scaffold to further aid in the development of bNOS-specific inhibitors. Targeting Bacterial Nitric Oxide Synthase with Aminoquinoline-based Inhibitors.,Holden JK, Lewis MC, Cinelli MA, Abdullatif Z, Pensa AV, Silverman RB, Poulos TL Biochemistry. 2016 Sep 8. PMID:27607918[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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