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==Crystal structure of an oxidoreductase from Mycobacterium smegmatis==
==Crystal structure of an oxidoreductase from Mycobacterium smegmatis==
<StructureSection load='3u0b' size='340' side='right' caption='[[3u0b]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='3u0b' size='340' side='right'caption='[[3u0b]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3u0b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_smegmatis Mycobacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U0B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U0B FirstGlance]. <br>
<table><tr><td colspan='2'>[[3u0b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U0B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U0B FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.7&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MSMEG_0372 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1772 Mycobacterium smegmatis])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=3u0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u0b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u0b RCSB], [http://www.ebi.ac.uk/pdbsum/3u0b PDBsum]</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=3u0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u0b OCA], [https://pdbe.org/3u0b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u0b RCSB], [https://www.ebi.ac.uk/pdbsum/3u0b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u0b ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0QPE7_MYCS2 A0QPE7_MYCS2]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The rise in antimicrobial resistance is a global health crisis and necessitates the development of novel strategies to treat infections. For example, in 2022 tuberculosis (TB) was the second leading infectious killer after COVID-19, with multi-drug-resistant strains of TB having an approximately 40% fatality rate. Targeting essential biosynthetic pathways in pathogens has proven to be successful for the development of novel antimicrobial treatments. Fatty-acid synthesis (FAS) in bacteria proceeds via the type II pathway, which is substantially different from the type I pathway utilized in animals. This makes bacterial fatty-acid biosynthesis (Fab) enzymes appealing as drug targets. FabG is an essential FASII enzyme, and some bacteria, such as Mycobacterium tuberculosis, the causative agent of TB, harbor multiple homologs. FabG4 is a conserved, high-molecular-weight FabG (HMwFabG) that was first identified in M. tuberculosis and is distinct from the canonical low-molecular-weight FabG. Here, structural and functional analyses of Mycolicibacterium smegmatis FabG4, the third HMwFabG studied to date, are reported. Crystal structures of NAD(+) and apo MsFabG4, along with kinetic analyses, show that MsFabG4 preferentially binds and uses NADH when reducing CoA substrates. As M. smegmatis is often used as a model organism for M. tuberculosis, these studies may aid the development of drugs to treat TB and add to the growing body of research that distinguish HMwFabGs from the archetypal low-molecular-weight FabG.
Structural and functional characterization of FabG4 from Mycolicibacterium smegmatis.,Ran X, Parikh P, Abendroth J, Arakaki TL, Clifton MC, Edwards TE, Lorimer DD, Mayclin S, Staker BL, Myler P, McLaughlin KJ Acta Crystallogr F Struct Biol Commun. 2024 Apr 1;80(Pt 4):82-91. doi: , 10.1107/S2053230X2400356X. Epub 2024 Apr 24. PMID:38656226<ref>PMID:38656226</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3u0b" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Mycobacterium smegmatis]]
[[Category: Large Structures]]
[[Category: Abendroth, J]]
[[Category: Mycolicibacterium smegmatis MC2 155]]
[[Category: Arakaki, T L]]
[[Category: Abendroth J]]
[[Category: Clifton, M]]
[[Category: Arakaki TL]]
[[Category: Structural genomic]]
[[Category: Clifton MC]]
[[Category: Staker, B L]]
[[Category: Staker BL]]
[[Category: Oxidoreductase]]
[[Category: Ssgcid]]
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