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| | ==Structure of the prenyltransferase MoeN5 in complex with geranyl pyrophosphate== | | ==Structure of the prenyltransferase MoeN5 in complex with geranyl pyrophosphate== |
| - | <StructureSection load='5b00' size='340' side='right' caption='[[5b00]], [[Resolution|resolution]] 2.95Å' scene=''> | + | <StructureSection load='5b00' size='340' side='right'caption='[[5b00]], [[Resolution|resolution]] 2.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5b00]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14672 Atcc 14672]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B00 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B00 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5b00]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_viridosporus Streptomyces viridosporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B00 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GPP:GERANYL+DIPHOSPHATE'>GPP</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GPP:GERANYL+DIPHOSPHATE'>GPP</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b01|5b01]], [[5b02|5b02]], [[5b03|5b03]]</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=5b00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b00 OCA], [https://pdbe.org/5b00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b00 RCSB], [https://www.ebi.ac.uk/pdbsum/5b00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b00 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">moeN5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=35758 ATCC 14672])</td></tr>
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| - | <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=5b00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b00 OCA], [http://pdbe.org/5b00 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b00 RCSB], [http://www.ebi.ac.uk/pdbsum/5b00 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b00 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A010_STRVD A0A010_STRVD] |
| | <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: Atcc 14672]] | + | [[Category: Large Structures]] |
| - | [[Category: Chen, C C]] | + | [[Category: Streptomyces viridosporus]] |
| - | [[Category: Guo, R T]] | + | [[Category: Chen C-C]] |
| - | [[Category: Ko, T P]] | + | [[Category: Guo R-T]] |
| - | [[Category: Zhang, L]] | + | [[Category: Ko T-P]] |
| - | [[Category: Alpha-helical fold]]
| + | [[Category: Zhang L]] |
| - | [[Category: Prenyltransferase]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
A0A010_STRVD
Publication Abstract from PubMed
The structure of MoeN5, a unique prenyltransferase involved in the biosynthesis of the antibiotic moenomycin, is reported. MoeN5 catalyzes the reaction of geranyl diphosphate (GPP) with the cis-farnesyl group in phosphoglycolipid 5 to form the (C25 ) moenocinyl-sidechain-containing lipid 7. GPP binds to an allylic site (S1) and aligns well with known S1 inhibitors. Alkyl glycosides, glycolipids, can bind to both S1 and a second site, S2. Long sidechains in S2 are "bent" and co-locate with the homoallylic substrate isopentenyl diphosphate in other prenyltransferases. These observations support a MoeN5 mechanism in which 5 binds to S2 with its C6-C11 group poised to attack C1 in GPP to form the moenocinyl sidechain, with the more distal regions of 5 aligning with the distal glucose in decyl maltoside. The results are of general interest because they provide the first structures of MoeN5 and a structural basis for its mechanism of action, results that will facilitate the design of new antibiotics.
Moenomycin Biosynthesis: Structure and Mechanism of Action of the Prenyltransferase MoeN5.,Zhang L, Chen CC, Ko TP, Huang JW, Zheng Y, Liu W, Wang I, Malwal SR, Feng X, Wang K, Huang CH, Hsu ST, Wang AH, Oldfield E, Guo RT Angew Chem Int Ed Engl. 2016 Apr 4;55(15):4716-20. doi: 10.1002/anie.201511388., Epub 2016 Mar 8. PMID:26954060[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang L, Chen CC, Ko TP, Huang JW, Zheng Y, Liu W, Wang I, Malwal SR, Feng X, Wang K, Huang CH, Hsu ST, Wang AH, Oldfield E, Guo RT. Moenomycin Biosynthesis: Structure and Mechanism of Action of the Prenyltransferase MoeN5. Angew Chem Int Ed Engl. 2016 Apr 4;55(15):4716-20. doi: 10.1002/anie.201511388., Epub 2016 Mar 8. PMID:26954060 doi:http://dx.doi.org/10.1002/anie.201511388
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