|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='4d3d' size='340' side='right'caption='[[4d3d]], [[Resolution|resolution]] 1.71Å' scene=''> | | <StructureSection load='4d3d' size='340' side='right'caption='[[4d3d]], [[Resolution|resolution]] 1.71Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4d3d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14579 Atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D3D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D3D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4d3d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D3D FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=P4C:O-ACETALDEHYDYL-HEXAETHYLENE+GLYCOL'>P4C</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]] 1.71Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d3f|4d3f]], [[4d3s|4d3s]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=P4C:O-ACETALDEHYDYL-HEXAETHYLENE+GLYCOL'>P4C</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </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=4d3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d3d OCA], [https://pdbe.org/4d3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d3d RCSB], [https://www.ebi.ac.uk/pdbsum/4d3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d3d 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=4d3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d3d OCA], [http://pdbe.org/4d3d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d3d RCSB], [http://www.ebi.ac.uk/pdbsum/4d3d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d3d ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| Line 22: |
Line 21: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 14579]] | + | [[Category: Bacillus cereus]] |
| - | [[Category: Dihydrofolate reductase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Grogan, G]] | + | [[Category: Grogan G]] |
| - | [[Category: Hart, S]] | + | [[Category: Hart S]] |
| - | [[Category: Man, H]] | + | [[Category: Man H]] |
| - | [[Category: Turkenburg, J P]] | + | [[Category: Turkenburg JP]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Sired]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Oxidoreductases from Streptomyces sp. GF3546 [3546-IRED], Bacillus cereus BAG3X2 (BcIRED) and Nocardiopsis halophila (NhIRED) each reduce prochiral 2-methylpyrroline (2MPN) to (S)-2-methylpyrrolidine with >95 % ee and also a number of other imine substrates with good selectivity. Structures of BcIRED and NhIRED have helped to identify conserved active site residues within this subgroup of imine reductases that have S selectivity towards 2MPN, including a tyrosine residue that has a possible role in catalysis and superimposes with an aspartate in related enzymes that display R selectivity towards the same substrate. Mutation of this tyrosine residue-Tyr169-in 3546-IRED to Phe resulted in a mutant of negligible activity. The data together provide structural evidence for the location and significance of the Tyr residue in this group of imine reductases, and permit a comparison of the active sites of enzymes that reduce 2MPN with either R or S selectivity.
Structure, Activity and Stereoselectivity of NADPH-Dependent Oxidoreductases Catalysing the S-Selective Reduction of the Imine Substrate 2-Methylpyrroline.,Man H, Wells E, Hussain S, Leipold F, Hart S, Turkenburg JP, Turner NJ, Grogan G Chembiochem. 2015 Mar 24. doi: 10.1002/cbic.201402625. PMID:25809902[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Man H, Wells E, Hussain S, Leipold F, Hart S, Turkenburg JP, Turner NJ, Grogan G. Structure, Activity and Stereoselectivity of NADPH-Dependent Oxidoreductases Catalysing the S-Selective Reduction of the Imine Substrate 2-Methylpyrroline. Chembiochem. 2015 Mar 24. doi: 10.1002/cbic.201402625. PMID:25809902 doi:http://dx.doi.org/10.1002/cbic.201402625
|
