5emh
From Proteopedia
(Difference between revisions)
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<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=5emh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5emh OCA], [http://pdbe.org/5emh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5emh RCSB], [http://www.ebi.ac.uk/pdbsum/5emh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5emh ProSAT]</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=5emh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5emh OCA], [http://pdbe.org/5emh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5emh RCSB], [http://www.ebi.ac.uk/pdbsum/5emh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5emh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Iridoid synthases belong to the family of short-chain dehydrogenase/reductase involved in the biosynthesis of iridoids. Despite having high sequence and structural homology with progesterone 5beta-reductase, these enzymes exhibit differential substrate specificities. Previously, two loops, L1 and L2 at substrate-binding pocket, were suggested to be involved in generating substrate specificity. However, the structural basis of specificity determinants was elusive. Here, combining sequence and structural analysis, site-directed mutagenesis, and molecular dynamics simulations, we have shown that iridoid synthase contains two channels for substrate entry whose geometries are altered by L1-L2 dynamics, primarily orchestrated by interactions of residues Glu161 and Gly162 of L1 and Asn358 of L2. A complex interplay of these interactions confer the substrate specificity to the enzyme. | ||
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| + | Dynamics of loops at the substrate entry channel determine the specificity of iridoid synthases.,Sandholu AS, Mohole M, Duax WL, Thulasiram HV, Sengupta D, Kulkarni K FEBS Lett. 2018 Aug;592(15):2624-2635. doi: 10.1002/1873-3468.13174. Epub 2018, Jul 10. PMID:29944733<ref>PMID:29944733</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5emh" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:32, 26 September 2018
Crystal structure of Iridoid Synthase from Cantharanthus roseus in complex with NADP+
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