|
|
| Line 1: |
Line 1: |
| | | | |
| | ==The structure of the H302A mutant of StlD== | | ==The structure of the H302A mutant of StlD== |
| - | <StructureSection load='5gk2' size='340' side='right' caption='[[5gk2]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='5gk2' size='340' side='right'caption='[[5gk2]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gk2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pholl Pholl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GK2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GK2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gk2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Photorhabdus_laumondii_subsp._laumondii_TTO1 Photorhabdus laumondii subsp. laumondii TTO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GK2 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gk0|5gk0]], [[5gk1|5gk1]]</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]] 2.201Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">plu2164 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243265 PHOLL])</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=5gk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gk2 OCA], [https://pdbe.org/5gk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gk2 RCSB], [https://www.ebi.ac.uk/pdbsum/5gk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gk2 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=5gk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gk2 OCA], [http://pdbe.org/5gk2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gk2 RCSB], [http://www.ebi.ac.uk/pdbsum/5gk2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gk2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q7N4Z6_PHOLL Q7N4Z6_PHOLL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pholl]] | + | [[Category: Large Structures]] |
| - | [[Category: Abe, I]] | + | [[Category: Photorhabdus laumondii subsp. laumondii TTO1]] |
| - | [[Category: Dngfeng, Y]] | + | [[Category: Abe I]] |
| - | [[Category: Mori, T]] | + | [[Category: Dngfeng Y]] |
| - | [[Category: Morita, H]] | + | [[Category: Mori T]] |
| - | [[Category: Ketosynthase]]
| + | [[Category: Morita H]] |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q7N4Z6_PHOLL
Publication Abstract from PubMed
In contrast to stilbene biosynthesis by type III polyketide synthase in plants, in bacteria stilbene is produced by the collaboration of two enzymes in Photorhabdus luminescens: the unusual beta-ketosynthase StlD catalyzes the condensation of the beta-ketoacyl starter with an alpha,beta-unsaturated-acyl substrate (two C-C bond-forming reactions) to produce isopropylstyrylcyclohexanedione, which is subsequently converted to stilbene by the aromatase StlC. Here we report the in vitro characterizations of StlD and StlC, and the X-ray crystal structures of StlD. Interestingly, structure-based mutagenesis demonstrated that His302, within the conserved Cys-His-Asn triad, is not essential for the enzyme reaction, while Glu154 functions as a base-catalyst to activate the beta-ketoacyl intermediate bound to the catalytic Cys126. The structures also revealed the presence of a putative nucleophilic water molecule activated by hydrogen bond networks with Glu154 and Ser340, suggesting that StlD employs novel catalytic machinery for the condensation of two acyl substrates to produce the cyclohexanedione scaffold.
Structural Insight into the Enzymatic Formation of Bacterial Stilbene.,Mori T, Awakawa T, Shimomura K, Saito Y, Yang D, Morita H, Abe I Cell Chem Biol. 2016 Dec 22;23(12):1468-1479. doi:, 10.1016/j.chembiol.2016.10.010. Epub 2016 Nov 17. PMID:27866911[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mori T, Awakawa T, Shimomura K, Saito Y, Yang D, Morita H, Abe I. Structural Insight into the Enzymatic Formation of Bacterial Stilbene. Cell Chem Biol. 2016 Dec 22;23(12):1468-1479. doi:, 10.1016/j.chembiol.2016.10.010. Epub 2016 Nov 17. PMID:27866911 doi:http://dx.doi.org/10.1016/j.chembiol.2016.10.010
|
