3m1l

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Current revision (08:31, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3m1l' size='340' side='right'caption='[[3m1l]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
<StructureSection load='3m1l' size='340' side='right'caption='[[3m1l]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3m1l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M1L FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3m1l]] is a 2 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=3M1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M1L FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.52&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv0242c ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3m1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m1l OCA], [https://pdbe.org/3m1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m1l RCSB], [https://www.ebi.ac.uk/pdbsum/3m1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m1l 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=3m1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m1l OCA], [https://pdbe.org/3m1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m1l RCSB], [https://www.ebi.ac.uk/pdbsum/3m1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m1l ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/O53665_MYCTO O53665_MYCTO]
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Rv0242c, also known as FabG4, is a beta-ketoacyl CoA reductase in Mycobacterium tuberculosis. The crystal structure of C-terminal truncated FabG4 is solved at 2.5A resolution which shows the presence of two distinct domains, domain I and II. Domain I partially resembles "flavodoxin type domain" and the domain II is a typical "ketoacyl CoA reductase (KAR) domain". The enzyme exhibits ketoacyl CoA reductase activity by reducing acetoacyl CoA to 3-hydroxyacyl CoA in presence of NADH. Conserved catalytic triad Ser347, Tyr360, and Lys364 constitute the active site residues of the KAR domain. Presence of the Tyr and the Lys residues in the triad in a particular orientation is imperative for effective catalytic mechanism. The importance of loop I and II and the role of the C-terminal residues of KAR domain are highlighted. Comparative structural analyses clearly demonstrate that loop II is stabilized by hydrophobic interaction with C-terminal residues to sustain the orientation of Tyr360. Loop I interacts with loop II via H-bonding network to restrict the active site residue Lys364 in a catalytically favorable orientation.
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Crystal structure of FabG4 from Mycobacterium tuberculosis reveals the importance of C-terminal residues in ketoreductase activity.,Dutta D, Bhattacharyya S, Mukherjee S, Saha B, Das AK J Struct Biol. 2010 Nov 21. PMID:21081168<ref>PMID:21081168</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3m1l" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Myctu]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Bhattacharyya, S]]
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[[Category: Bhattacharyya S]]
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[[Category: Das, A K]]
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[[Category: Das AK]]
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[[Category: Dutta, D]]
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[[Category: Dutta D]]
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[[Category: Saha, B]]
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[[Category: Saha B]]
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[[Category: Ketoacyl reductase]]
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[[Category: Oxidoreductase]]
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[[Category: Rossmann fold]]
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[[Category: Short chain dehydrogenase]]
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Current revision

Crystal structure of a C-terminal trunacted mutant of a putative ketoacyl reductase (FabG4) from Mycobacterium tuberculosis H37Rv at 2.5 Angstrom resolution

PDB ID 3m1l

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