4rv2: Difference between revisions
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==Crystal Structure of (3R)-hydroxyacyl-ACP dehydratase HadAB hetero-dimer from Mycobacterium smegmatis== | ==Crystal Structure of (3R)-hydroxyacyl-ACP dehydratase HadAB hetero-dimer from Mycobacterium smegmatis== | ||
<StructureSection load='4rv2' size='340' side='right' caption='[[4rv2]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='4rv2' size='340' side='right' caption='[[4rv2]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
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<table><tr><td colspan='2'>[[4rv2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RV2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RV2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4rv2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RV2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RV2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4rv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rv2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rv2 RCSB], [http://www.ebi.ac.uk/pdbsum/4rv2 PDBsum]</span></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=4rv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rv2 OCA], [http://pdbe.org/4rv2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rv2 RCSB], [http://www.ebi.ac.uk/pdbsum/4rv2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rv2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4rv2" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 04:10, 19 January 2017
Crystal Structure of (3R)-hydroxyacyl-ACP dehydratase HadAB hetero-dimer from Mycobacterium smegmatisCrystal Structure of (3R)-hydroxyacyl-ACP dehydratase HadAB hetero-dimer from Mycobacterium smegmatis
Structural highlights
Publication Abstract from PubMedFatty acid biosynthesis type II in mycobacteria delivers the fatty acids required for mycolic acid synthesis. The pathway employs a unique maoC like beta-hydroxyacyl-ACP dehydratase HadAB or HadBC heterodimer in the third step of the elongation cycle. Here we report the crystal structure of the HadAB complex determined using a Pb-SIRAS method. Crystal structure aided with enzymatic study establishes the roles of HadA as a scaffolding component and HadB as a catalytic component together indispensable for the activity. The detailed structural analysis of HadAB in combination with MD simulation endorses the spatial orientation of the central hot-dog helix and the dynamic nature of its associated loop in regulation of substrate specificities in dehydratase/hydratase family enzymes. Crystal structure of dehydratase component HadAB complex of mycobacterial FAS-II pathway.,Biswas R, Dutta A, Dutta D, Hazra D, Banerjee DR, Basak A, Das AK Biochem Biophys Res Commun. 2015 Mar 6;458(2):369-74. doi:, 10.1016/j.bbrc.2015.01.119. Epub 2015 Feb 3. PMID:25656575[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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