View source for 6kj5


==Crystal structure of 10-Hydroxygeraniol Dehydrogenase apo form from Cantharanthus roseus==
<StructureSection load='6kj5' size='340' side='right'caption='[[6kj5]], [[Resolution|resolution]] 3.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6kj5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Catharanthus_roseus Catharanthus roseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KJ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KJ5 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]] 3.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6kj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kj5 OCA], [https://pdbe.org/6kj5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kj5 RCSB], [https://www.ebi.ac.uk/pdbsum/6kj5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kj5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/10HGO_CATRO 10HGO_CATRO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Conversion of 10-hydroxygeraniol to 10-oxogeranial is a crucial step in iridoid biosynthesis. This reaction is catalyzed by a zinc-dependent alcohol dehydrogenase, 10-hydroxygeraniol dehydrogenase, belonging to the family of medium-chain dehydrogenase/reductase (MDR). Here, we report the crystal structures of a novel 10-hydroxygeraniol dehydrogenase from Catharanthus roseus in its apo and nicotinamide adenine dinucleotide phosphate (NADP(+) ) bound forms. Structural analysis and docking studies reveal how subtle conformational differences of loops L1, L2, L3, and helix alpha9' at the orifice of the catalytic site confer differential activity of the enzyme toward various substrates, by modulating the binding pocket shape and volume. The present study, first of its kind, provides insights into the structural basis of substrate specificity of MDRs specific to linear substrates. Furthermore, comparison of apo and NADP(+) bound structures suggests that the enzyme adopts open and closed states to facilitate cofactor binding.

Structural studies on 10-hydroxygeraniol dehydrogenase: A novel linear substrate-specific dehydrogenase from Catharanthus roseus.,Sandholu AS, Mujawar SP, Ramakrishnan K, Thulasiram HV, Kulkarni K Proteins. 2020 Sep;88(9):1197-1206. doi: 10.1002/prot.25891. Epub 2020 Mar 26. PMID:32181958<ref>PMID:32181958</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6kj5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Catharanthus roseus]]
[[Category: Large Structures]]
[[Category: Kulkarni KA]]
[[Category: Sandholu AS]]
[[Category: Sharmila PM]]
[[Category: Thulasiram HV]]