5y4g
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Apo Structure of AmbP3== | |
| + | <StructureSection load='5y4g' size='340' side='right' caption='[[5y4g]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5y4g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y4G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y4G FirstGlance]. <br> | ||
| + | </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=5y4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y4g OCA], [http://pdbe.org/5y4g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y4g RCSB], [http://www.ebi.ac.uk/pdbsum/5y4g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y4g ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:29178634</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5y4g" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Awakawa, T]] | [[Category: Awakawa, T]] | ||
| - | [[Category: Wong, C | + | [[Category: Nakashima, Y]] |
| + | [[Category: Wong, C P]] | ||
| + | [[Category: Prenyltransferase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 07:30, 18 July 2018
Apo Structure of AmbP3
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