|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5y7c' size='340' side='right'caption='[[5y7c]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='5y7c' size='340' side='right'caption='[[5y7c]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5y7c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Fischerella_utex1903 Fischerella utex1903]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y7C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y7C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5y7c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fischerella_ambigua_UTEX_1903 Fischerella ambigua UTEX 1903]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y7C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8O0:Hapalindole+A'>8O0</scene>, <scene name='pdbligand=DST:DIMETHYLALLYL+S-THIOLODIPHOSPHATE'>DST</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]] 2.003Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ambP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=230521 Fischerella UTEX1903])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8O0:Hapalindole+A'>8O0</scene>, <scene name='pdbligand=DST:DIMETHYLALLYL+S-THIOLODIPHOSPHATE'>DST</scene></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=5y7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y7c OCA], [http://pdbe.org/5y7c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y7c RCSB], [http://www.ebi.ac.uk/pdbsum/5y7c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y7c 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=5y7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y7c OCA], [https://pdbe.org/5y7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y7c RCSB], [https://www.ebi.ac.uk/pdbsum/5y7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y7c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/V5TDY7_FISAU V5TDY7_FISAU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Fischerella utex1903]] | + | [[Category: Fischerella ambigua UTEX 1903]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Awakawa, T]] | + | [[Category: Awakawa T]] |
| - | [[Category: Nakashima, Y]] | + | [[Category: Nakashima Y]] |
| - | [[Category: Wong, C P]] | + | [[Category: Wong CP]] |
| - | [[Category: Prenyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
V5TDY7_FISAU
Publication Abstract from PubMed
The cyanobacterial prenyltransferase AmbP3 catalyzes the reverse prenylation of the tetracyclic indole alkaloid hapalindole U at its C-2 position. Interestingly, AmbP3 also accepts hapalindole A, a halogenated C-10 epimer of hapalindole U, and catalyzes normal prenylation at its C-2 position. The comparison of the two ternary crystal structures, AmbP3-DMSPP/hapalindole U and AmbP3-DMSPP/hapalindole A, at 1.65-2.00 A resolution revealed two distinct orientations for the substrate binding that define reverse or normal prenylation. The tolerance of the enzyme for these altered orientations is attributed to the hydrophobicity of the substrate binding pocket and the plasticity of the amino acids surrounding the allyl group of the prenyl donor. This is the first study to provide the intimate structural basis for the normal and reverse prenylations catalyzed by a single enzyme, and it offers novel insight into the engineered biosynthesis of prenylated natural products.
Two Distinct Substrate Binding Modes for the Normal and Reverse Prenylation of Hapalindoles by the Prenyltransferase AmbP3.,Wong CP, Awakawa T, Nakashima Y, Mori T, Zhu Q, Liu X, Abe I Angew Chem Int Ed Engl. 2018 Jan 8;57(2):560-563. doi: 10.1002/anie.201710682., Epub 2017 Dec 15. PMID:29178634[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wong CP, Awakawa T, Nakashima Y, Mori T, Zhu Q, Liu X, Abe I. Two Distinct Substrate Binding Modes for the Normal and Reverse Prenylation of Hapalindoles by the Prenyltransferase AmbP3. Angew Chem Int Ed Engl. 2018 Jan 8;57(2):560-563. doi: 10.1002/anie.201710682., Epub 2017 Dec 15. PMID:29178634 doi:http://dx.doi.org/10.1002/anie.201710682
|
