6m4q: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
Line 3: Line 3:
<StructureSection load='6m4q' size='340' side='right'caption='[[6m4q]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
<StructureSection load='6m4q' size='340' side='right'caption='[[6m4q]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6m4q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_spectabilis Streptomyces spectabilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M4Q FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M4Q FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35&#8491;</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]] 1.35&#8491;</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></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></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=6m4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m4q OCA], [https://pdbe.org/6m4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m4q RCSB], [https://www.ebi.ac.uk/pdbsum/6m4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m4q 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=6m4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m4q OCA], [https://pdbe.org/6m4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m4q RCSB], [https://www.ebi.ac.uk/pdbsum/6m4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m4q ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A286SBY7_STRST A0A286SBY7_STRST]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Streptovaricin C is a naphthalenic ansamycin antibiotic structurally similar to rifamycins with potential anti-MRSA bioactivities. However, the formation mechanism of the most fascinating and bioactivity-related methylenedioxy bridge (MDB) moiety in streptovaricins is unclear. Based on genetic and biochemical evidences, we herein clarify that the P450 enzyme StvP2 catalyzes the MDB formation in streptovaricins, with an atypical substrate inhibition kinetics. Furthermore, X-ray crystal structures in complex with substrate and structure-based mutagenesis reveal the intrinsic details of the enzymatic reaction. The mechanism of MDB formation is proposed to be an intramolecular nucleophilic substitution resulting from the hydroxylation by the heme core and the keto-enol tautomerization via a crucial catalytic triad (Asp89-His92-Arg72) in StvP2. In addition, in vitro reconstitution uncovers that C6-O-methylation and C4-O-acetylation of streptovaricins are necessary prerequisites for the MDB formation. This work provides insight for the MDB formation and adds evidence in support of the functional versatility of P450 enzymes.
Uncovering the cytochrome P450-catalyzed methylenedioxy bridge formation in streptovaricins biosynthesis.,Sun G, Hu C, Mei Q, Luo M, Chen X, Li Z, Liu Y, Deng Z, Zhang Z, Sun Y Nat Commun. 2020 Sep 9;11(1):4501. doi: 10.1038/s41467-020-18336-5. PMID:32908132<ref>PMID:32908132</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6m4q" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Streptomyces spectabilis]]
[[Category: Chen X]]
[[Category: Chen X]]
[[Category: Deng Z]]
[[Category: Deng Z]]

Latest revision as of 13:28, 13 August 2026

Cytochrome P450 monooxygenase StvP2 substrate-free structure

6m4q, resolution 1.35Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=6m4q&oldid=4479685"