6a52: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(One intermediate revision by the same user not shown)
Line 1: Line 1:


==Oxidase ChaP-H1==
==Oxidase ChaP-H1==
<StructureSection load='6a52' size='340' side='right' caption='[[6a52]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='6a52' size='340' side='right'caption='[[6a52]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6a52]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_44812 Dsm 44812]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A52 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6a52]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_phenolicus Rhodococcus phenolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A52 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></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]] 2&#8491;</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=6a52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a52 OCA], [http://pdbe.org/6a52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a52 RCSB], [http://www.ebi.ac.uk/pdbsum/6a52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a52 ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</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=6a52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a52 OCA], [https://pdbe.org/6a52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a52 RCSB], [https://www.ebi.ac.uk/pdbsum/6a52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a52 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/A0A3F2YLV5_9NOCA A0A3F2YLV5_9NOCA]
Oxidative rearrangements play key roles in introducing structural complexity and biological activities of natural products biosynthesized by type II polyketide synthases (PKSs). Chartreusin (1) is a potent antitumor polyketide that contains a unique rearranged pentacyclic aromatic bilactone aglycone derived from a type II PKS. Herein, we report an unprecedented dioxygenase, ChaP, that catalyzes the final alpha-pyrone ring formation in 1 biosynthesis using flavin-activated oxygen as an oxidant. The X-ray crystal structures of ChaP and two homologues, docking studies, and site-directed mutagenesis provided insights into the molecular basis of the oxidative rearrangement that involves two successive C-C bond cleavage steps followed by lactonization. ChaP is the first example of a dioxygenase that requires a flavin-activated oxygen as a substrate despite lacking flavin binding sites, and represents a new class in the vicinal oxygen chelate enzyme superfamily.
 
Molecular Basis for the Final Oxidative Rearrangement Steps in Chartreusin Biosynthesis.,Wang YS, Zhang B, Zhu J, Yang CL, Guo Y, Liu CL, Liu F, Huang H, Zhao S, Liang Y, Jiao RH, Tan RX, Ge HM J Am Chem Soc. 2018 Aug 15. doi: 10.1021/jacs.8b06623. PMID:30067334<ref>PMID:30067334</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6a52" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Dsm 44812]]
[[Category: Large Structures]]
[[Category: Ge, H M]]
[[Category: Rhodococcus phenolicus]]
[[Category: Zhang, B]]
[[Category: Ge HM]]
[[Category: Biosynthetic protein]]
[[Category: Zhang B]]
[[Category: Chartreusin]]
[[Category: Dimer]]
[[Category: Dioxygenase]]
[[Category: Oxidative rearrangement]]
[[Category: Voc family]]

Latest revision as of 13:30, 27 March 2024

Oxidase ChaP-H1Oxidase ChaP-H1

Structural highlights

6a52 is a 2 chain structure with sequence from Rhodococcus phenolicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A3F2YLV5_9NOCA

6a52, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=6a52&oldid=4112166"