5uhu: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5uhu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Micromonospora_griseorubida Micromonospora griseorubida]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UHU FirstGlance]. <br> | <table><tr><td colspan='2'>[[5uhu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Micromonospora_griseorubida Micromonospora griseorubida]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UHU FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, models</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MIV:MYCINAMICIN+IV'>MIV</scene></td></tr> | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MIV:MYCINAMICIN+IV'>MIV</scene></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=5uhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uhu OCA], [https://pdbe.org/5uhu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uhu RCSB], [https://www.ebi.ac.uk/pdbsum/5uhu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uhu 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=5uhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uhu OCA], [https://pdbe.org/5uhu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uhu RCSB], [https://www.ebi.ac.uk/pdbsum/5uhu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uhu ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/MYCG_MICGR MYCG_MICGR] Involved in the biosynthesis of mycinamicin, a 16-membered macrolide antibiotic. Catalyzes consecutive hydroxylation (at C14) and epoxidation (at C12-C13) reactions with mycinamicin IV as initial substrate, leading to mycinamicin II. These reactions require prior dimethylation of 6-deoxyallose to mycinose for effective conversion by the dual function MycG enzyme.<ref>PMID:18804032</ref> <ref>PMID:22547618</ref> <ref>PMID:7808395</ref> | [https://www.uniprot.org/uniprot/MYCG_MICGR MYCG_MICGR] Involved in the biosynthesis of mycinamicin, a 16-membered macrolide antibiotic. Catalyzes consecutive hydroxylation (at C14) and epoxidation (at C12-C13) reactions with mycinamicin IV as initial substrate, leading to mycinamicin II. These reactions require prior dimethylation of 6-deoxyallose to mycinose for effective conversion by the dual function MycG enzyme.<ref>PMID:18804032</ref> <ref>PMID:22547618</ref> <ref>PMID:7808395</ref> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
MycG is a P450 monooxygenase that catalyzes the sequential hydroxylation and epoxidation of mycinamicin IV (M-IV), the last two steps in the biosynthesis of mycinamicin II, a macrolide antibiotic isolated from Micromonospora griseorubida. The crystal structure of MycG with M-IV bound was previously determined but showed the bound substrate in an orientation that did not rationalize the observed regiochemistry of M-IV hydroxylation. Nuclear magnetic resonance paramagnetic relaxation enhancements provided evidence of an orientation of M-IV in the MycG active site more compatible with the observed chemistry, but substrate-induced changes in the enzyme structure were not characterized. We now describe the use of amide 1H-15N residual dipolar couplings as experimental restraints in solvated "soft annealing" molecular dynamics simulations to generate solution structural ensembles of M-IV-bound MycG. Chemical shift perturbations, hydrogen-deuterium exchange, and 15N relaxation behavior provide insight into the dynamic and electronic perturbations in the MycG structure in response to M-IV binding. The solution and crystallographic structures are compared, and the possibility that the crystallographic orientation of bound M-IV represents an inhibitory mode is discussed. | |||
Solution Conformations and Dynamics of Substrate-Bound Cytochrome P450 MycG.,Tietz DR, Podust LM, Sherman DH, Pochapsky TC Biochemistry. 2017 May 30;56(21):2701-2714. doi: 10.1021/acs.biochem.7b00291., Epub 2017 May 16. PMID:28488849<ref>PMID:28488849</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 5uhu" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
