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| | <StructureSection load='5emh' size='340' side='right'caption='[[5emh]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='5emh' size='340' side='right'caption='[[5emh]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5emh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Catro Catro]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EMH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5EMH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5emh]] 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=5EMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EMH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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]] 2.1Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Iridoid_synthase Iridoid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.99 1.3.1.99] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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'>[https://proteopedia.org/fgij/fg.htm?mol=5emh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5emh OCA], [https://pdbe.org/5emh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5emh RCSB], [https://www.ebi.ac.uk/pdbsum/5emh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5emh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/IRIS_CATRO IRIS_CATRO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Catro]] | + | [[Category: Catharanthus roseus]] |
| - | [[Category: Iridoid synthase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kulkarni, K A]] | + | [[Category: Kulkarni KA]] |
| - | [[Category: Sandholu, A]] | + | [[Category: Sandholu A]] |
| - | [[Category: Thulasiram, H V]] | + | [[Category: Thulasiram HV]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Nadph]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Reductase]]
| + | |
| Structural highlights
Function
IRIS_CATRO
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sandholu AS, Mohole M, Duax WL, Thulasiram HV, Sengupta D, Kulkarni K. Dynamics of loops at the substrate entry channel determine the specificity of iridoid synthases. FEBS Lett. 2018 Aug;592(15):2624-2635. doi: 10.1002/1873-3468.13174. Epub 2018, Jul 10. PMID:29944733 doi:http://dx.doi.org/10.1002/1873-3468.13174
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