4zqm: Difference between revisions

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 ==Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Mycobacterium tuberculosis in the complex with XMP and NAD==
-<StructureSection load='4zqm' size='340' side='right' caption='[[4zqm]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+<StructureSection load='4zqm' size='340' side='right'caption='[[4zqm]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4zqm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZQM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZQM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4zqm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZQM FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=XMP:XANTHOSINE-5-MONOPHOSPHATE'>XMP</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]] 1.602&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zqn|4zqn]], [[4zqo|4zqo]], [[4zqp|4zqp]], [[4zqr|4zqr]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=XMP:XANTHOSINE-5-MONOPHOSPHATE'>XMP</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=4zqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zqm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4zqm RCSB], [http://www.ebi.ac.uk/pdbsum/4zqm 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=4zqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zqm OCA], [https://pdbe.org/4zqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zqm RCSB], [https://www.ebi.ac.uk/pdbsum/4zqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zqm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/IMDH_MYCTU IMDH_MYCTU]] Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.[HAMAP-Rule:MF_01964]
+[https://www.uniprot.org/uniprot/IMDH_MYCTU IMDH_MYCTU] Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.[HAMAP-Rule:MF_01964]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Tuberculosis (TB) remains a worldwide problem and the need for new drugs is increasingly more urgent with the emergence of multidrug- and extensively-drug resistant TB. Inosine 5'-monophosphate dehydrogenase 2 (IMPDH2) from Mycobacterium tuberculosis (Mtb) is an attractive drug target. The enzyme catalyzes the conversion of inosine 5'-monophosphate into xanthosine 5'-monophosphate with the concomitant reduction of NAD+ to NADH. This reaction controls flux into the guanine nucleotide pool. We report seventeen selective IMPDH inhibitors with antitubercular activity. The crystal structures of a deletion mutant of MtbIMPDH2 in the apo form and in complex with the product XMP and substrate NAD+ are determined. We also report the structures of complexes with IMP and three structurally distinct inhibitors, including two with antitubercular activity. These structures will greatly facilitate the development of MtbIMPDH2-targeted antibiotics.
+Mycobacterium tuberculosis IMPDH in Complexes with Substrates, Products and Antitubercular Compounds.,Makowska-Grzyska M, Kim Y, Gorla SK, Wei Y, Mandapati K, Zhang M, Maltseva N, Modi G, Boshoff HI, Gu M, Aldrich C, Cuny GD, Hedstrom L, Joachimiak A PLoS One. 2015 Oct 6;10(10):e0138976. doi: 10.1371/journal.pone.0138976., eCollection 2015. PMID:26440283<ref>PMID:26440283</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4zqm" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Inosine monophosphate dehydrogenase 3D structures|Inosine monophosphate dehydrogenase 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
-[[Category: Andesrson, W F]]
+[[Category: Large Structures]]
-[[Category: Structural genomic]]
+[[Category: Mycobacterium tuberculosis H37Rv]]
-[[Category: Gu, M]]
+[[Category: Anderson WF]]
-[[Category: Hedstrom, L]]
+[[Category: Gu M]]
-[[Category: Joachimiak, A]]
+[[Category: Hedstrom L]]
-[[Category: Kavitha, M]]
+[[Category: Joachimiak A]]
-[[Category: Kim, Y]]
+[[Category: Kavitha M]]
-[[Category: Makowska-Grzyska, M]]
+[[Category: Kim Y]]
-[[Category: Maltseva, N]]
+[[Category: Makowska-Grzyska M]]
-[[Category: Csgid]]
+[[Category: Maltseva N]]
-[[Category: Delta-cb]]
-[[Category: Impdh]]
-[[Category: Mycobacterium tuberculosis]]