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==Radical SAM 1,2-diol dehydratase AprD4 in complex with its substrate paromamine== | |||
<StructureSection load='6fd2' size='340' side='right' caption='[[6fd2]], [[Resolution|resolution]] 2.55Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6fd2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FD2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FD2 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5AD:5-DEOXYADENOSINE'>5AD</scene>, <scene name='pdbligand=D5E:paromamine'>D5E</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=6fd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fd2 OCA], [http://pdbe.org/6fd2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fd2 RCSB], [http://www.ebi.ac.uk/pdbsum/6fd2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fd2 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Regiospecific dehydration of vicinal diols by enzymes is a difficult reaction that usually requires activation by dedicated organic cofactors. The enzymatic use of radical-based chemistry is an effective but challenging alternative as radical intermediates are difficult to control. Here we report the X-ray structure of the radical S-adenosyl-L-methionine (SAM) dehydratase AprD4 involved in the biosynthesis of the aminoglycoside (AG) antibiotic apramycin. Using in vitro characterizations and theoretical calculations based on our crystal structure, we have been able to propose a detailed mechanism of AprD4 catalysis, which involves a complex partially substrate-induced proton relay network in the enzyme active site and highlights the key role of the protein matrix in driving high-energy intermediates. | |||
1,2-diol dehydration by the radical SAM enzyme AprD4 - a matter of proton circulation and substrate flexibility.,Liu WQ, Amara P, Mouesca JM, Ji X, Renoux O, Martin L, Zhang C, Zhang Q, Nicolet Y J Am Chem Soc. 2018 Jan 4. doi: 10.1021/jacs.7b10501. PMID:29300094<ref>PMID:29300094</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6fd2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Amara, P]] | |||
[[Category: Ji, X]] | |||
[[Category: Liu, W Q]] | |||
[[Category: Martin, L]] | [[Category: Martin, L]] | ||
[[Category: | [[Category: Mouesca, J M]] | ||
[[Category: Nicolet, Y]] | [[Category: Nicolet, Y]] | ||
[[Category: Renoux, O]] | [[Category: Renoux, O]] | ||
[[Category: Zhang, C]] | [[Category: Zhang, C]] | ||
[[Category: Zhang, Q]] | [[Category: Zhang, Q]] | ||
[[Category: 2-diol dehydratase]] | |||
[[Category: Biosynthetic protein]] | |||
[[Category: Fes-cluster containing enzyme]] | |||
[[Category: Radical sam]] | |||
Revision as of 10:12, 17 January 2018
Radical SAM 1,2-diol dehydratase AprD4 in complex with its substrate paromamineRadical SAM 1,2-diol dehydratase AprD4 in complex with its substrate paromamine
Structural highlights
Publication Abstract from PubMedRegiospecific dehydration of vicinal diols by enzymes is a difficult reaction that usually requires activation by dedicated organic cofactors. The enzymatic use of radical-based chemistry is an effective but challenging alternative as radical intermediates are difficult to control. Here we report the X-ray structure of the radical S-adenosyl-L-methionine (SAM) dehydratase AprD4 involved in the biosynthesis of the aminoglycoside (AG) antibiotic apramycin. Using in vitro characterizations and theoretical calculations based on our crystal structure, we have been able to propose a detailed mechanism of AprD4 catalysis, which involves a complex partially substrate-induced proton relay network in the enzyme active site and highlights the key role of the protein matrix in driving high-energy intermediates. 1,2-diol dehydration by the radical SAM enzyme AprD4 - a matter of proton circulation and substrate flexibility.,Liu WQ, Amara P, Mouesca JM, Ji X, Renoux O, Martin L, Zhang C, Zhang Q, Nicolet Y J Am Chem Soc. 2018 Jan 4. doi: 10.1021/jacs.7b10501. PMID:29300094[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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