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| | ==Crystal structure of prenyltransferase AmbP1 apo structure== | | ==Crystal structure of prenyltransferase AmbP1 apo structure== |
| - | <StructureSection load='5z43' size='340' side='right' caption='[[5z43]], [[Resolution|resolution]] 2.36Å' scene=''> | + | <StructureSection load='5z43' size='340' side='right'caption='[[5z43]], [[Resolution|resolution]] 2.36Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5z43]] 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=5Z43 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z43 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5z43]] 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=5Z43 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Z43 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></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]] 2.361Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ambP1, famD2 ([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=MG:MAGNESIUM+ION'>MG</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=5z43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z43 OCA], [http://pdbe.org/5z43 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z43 RCSB], [http://www.ebi.ac.uk/pdbsum/5z43 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z43 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=5z43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z43 OCA], [https://pdbe.org/5z43 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5z43 RCSB], [https://www.ebi.ac.uk/pdbsum/5z43 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5z43 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/V5TDZ4_FISAU V5TDZ4_FISAU] |
| | <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: Fischerella utex1903]] | + | [[Category: Fischerella ambigua UTEX 1903]] |
| - | [[Category: Abe, I]] | + | [[Category: Large Structures]] |
| - | [[Category: Awakawa, T]] | + | [[Category: Abe I]] |
| - | [[Category: Mori, T]] | + | [[Category: Awakawa T]] |
| - | [[Category: Nakashima, Y]] | + | [[Category: Mori T]] |
| - | [[Category: Ambp1]]
| + | [[Category: Nakashima Y]] |
| - | [[Category: Indole]]
| + | |
| - | [[Category: Prenyltransferase]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
V5TDZ4_FISAU
Publication Abstract from PubMed
AmbP1 is a cyanobacterial aromatic prenyltransferase and a dedicated synthase for (R)-3-geranyl-3-isocyanovinyl indolenine (2), the biogenetic precursor for hapalindole-type alkaloids. The regioselective geranylation of cis-indolyl vinyl isonitrile (1) by the standalone AmbP1 to give 2 has been shown to require a magnesium ion (Mg(2+) ) to suppress the formation of cis-2-geranylindolyl vinyl isonitrile (3). Here, we report high-resolution crystal structures of AmbP1 in complex with 1 and geranyl S-thiodiphosphate (GSPP) in the presence and absence of a Mg(2+) effector. The comparative study of these structures revealed a unique allosteric binding site for Mg(2+) that modulates the conformation of 1 in the active site of AmbP1 for its selective geranylation. This work defines the structural basis for AmbP1 catalysis in the biogenesis of hapalindole-type alkaloids and provides the first atomic-level insight to the allosteric regulation of prenyltransferases.
Molecular Insight into the Mg(2+) -Dependent Allosteric Control of Indole Prenylation by Aromatic Prenyltransferase AmbP1.,Awakawa T, Mori T, Nakashima Y, Zhai R, Wong CP, Hillwig ML, Liu X, Abe I Angew Chem Int Ed Engl. 2018 Jun 4;57(23):6810-6813. doi: 10.1002/anie.201800855., Epub 2018 May 7. PMID:29677386[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Awakawa T, Mori T, Nakashima Y, Zhai R, Wong CP, Hillwig ML, Liu X, Abe I. Molecular Insight into the Mg(2+) -Dependent Allosteric Control of Indole Prenylation by Aromatic Prenyltransferase AmbP1. Angew Chem Int Ed Engl. 2018 Jun 4;57(23):6810-6813. doi: 10.1002/anie.201800855., Epub 2018 May 7. PMID:29677386 doi:http://dx.doi.org/10.1002/anie.201800855
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