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< | ==Structure of Mycobacterium smegmatis putative reductase MS0308== | ||
<StructureSection load='2xw7' size='340' side='right'caption='[[2xw7]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xw7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis Mycolicibacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XW7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XW7 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]] 2Å</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>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=2xw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xw7 OCA], [https://pdbe.org/2xw7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xw7 RCSB], [https://www.ebi.ac.uk/pdbsum/2xw7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xw7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0QP85_MYCS2 A0QP85_MYCS2] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Mycobacterium tuberculosis, the most successful bacterial pathogen, causes tuberculosis, a disease that still causes more than 2 million deaths per year. Arylamine N-acetyltransferase is an enzyme that is conserved in most Mycobacterium spp. The nat gene belongs to an operon that is important for the intracellular survival of M. tuberculosis within macrophages. The nat operon in Mycobacterium smegmatis and other fast-growing mycobacterial species has a unique organization containing genes with uncharacterized function. Here, we describe the biochemical, biophysical and structural characterization of the MSMEG_0308 gene product (MS0308) of the M. smegmatis nat operon. While characterizing the function of MS0308, we validated the oxidoreductase property; however, we found that the enzyme was not utilizing dihydrofolate as its substrate, hence we first report that MS0308 is not a dihydrofolate reductase, as annotated in the genome. The structure of this oxidoreductase was solved at 2.0 A in complex with the cofactor NADPH and has revealed the hydrophobic pocket where the endogenous substrate binds. | |||
Characterization of an oxidoreductase from the arylamine N-acetyltransferase operon in Mycobacterium smegmatis.,Evangelopoulos D, Cronin N, Daviter T, Sim E, Keep NH, Bhakta S FEBS J. 2011 Dec;278(24):4824-32. doi: 10.1111/j.1742-4658.2011.08382.x. Epub, 2011 Oct 31. PMID:21972977<ref>PMID:21972977</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2xw7" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Dihydrofolate reductase 3D structures|Dihydrofolate reductase 3D structures]] | |||
[[Category: | == References == | ||
[[Category: Bhakta | <references/> | ||
[[Category: Cronin | __TOC__ | ||
[[Category: Daviter | </StructureSection> | ||
[[Category: Evangelopoulos | [[Category: Large Structures]] | ||
[[Category: Gupta | [[Category: Mycolicibacterium smegmatis]] | ||
[[Category: Keep | [[Category: Bhakta S]] | ||
[[Category: Lack | [[Category: Cronin N]] | ||
[[Category: Sim | [[Category: Daviter T]] | ||
[[Category: Evangelopoulos D]] | |||
[[Category: Gupta A]] | |||
[[Category: Keep NH]] | |||
[[Category: Lack N]] | |||
[[Category: Sim E]] | |||
Latest revision as of 13:40, 20 December 2023
Structure of Mycobacterium smegmatis putative reductase MS0308Structure of Mycobacterium smegmatis putative reductase MS0308
Structural highlights
FunctionPublication Abstract from PubMedMycobacterium tuberculosis, the most successful bacterial pathogen, causes tuberculosis, a disease that still causes more than 2 million deaths per year. Arylamine N-acetyltransferase is an enzyme that is conserved in most Mycobacterium spp. The nat gene belongs to an operon that is important for the intracellular survival of M. tuberculosis within macrophages. The nat operon in Mycobacterium smegmatis and other fast-growing mycobacterial species has a unique organization containing genes with uncharacterized function. Here, we describe the biochemical, biophysical and structural characterization of the MSMEG_0308 gene product (MS0308) of the M. smegmatis nat operon. While characterizing the function of MS0308, we validated the oxidoreductase property; however, we found that the enzyme was not utilizing dihydrofolate as its substrate, hence we first report that MS0308 is not a dihydrofolate reductase, as annotated in the genome. The structure of this oxidoreductase was solved at 2.0 A in complex with the cofactor NADPH and has revealed the hydrophobic pocket where the endogenous substrate binds. Characterization of an oxidoreductase from the arylamine N-acetyltransferase operon in Mycobacterium smegmatis.,Evangelopoulos D, Cronin N, Daviter T, Sim E, Keep NH, Bhakta S FEBS J. 2011 Dec;278(24):4824-32. doi: 10.1111/j.1742-4658.2011.08382.x. Epub, 2011 Oct 31. PMID:21972977[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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