4xrt
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xrt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_steffisburgensis Streptomyces steffisburgensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XRT FirstGlance]. <br> | <table><tr><td colspan='2'>[[4xrt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_steffisburgensis Streptomyces steffisburgensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XRT FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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]] 1.952Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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=4xrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xrt OCA], [https://pdbe.org/4xrt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xrt RCSB], [https://www.ebi.ac.uk/pdbsum/4xrt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xrt 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=4xrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xrt OCA], [https://pdbe.org/4xrt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xrt RCSB], [https://www.ebi.ac.uk/pdbsum/4xrt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xrt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q2PA00_9ACTN Q2PA00_9ACTN] | [https://www.uniprot.org/uniprot/Q2PA00_9ACTN Q2PA00_9ACTN] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Aromatic polyketides make up a large class of natural products with diverse bioactivity. During biosynthesis, linear poly-beta-ketone intermediates are regiospecifically cyclized, yielding molecules with defined cyclization patterns that are crucial for polyketide bioactivity. The aromatase/cyclases (ARO/CYCs) are responsible for regiospecific cyclization of bacterial polyketides. The two most common cyclization patterns are C7-C12 and C9-C14 cyclizations. We have previously characterized three monodomain ARO/CYCs: ZhuI, TcmN, and WhiE. The last remaining uncharacterized class of ARO/CYCs is the di-domain ARO/CYCs, which catalyze C7-C12 cyclization and/or aromatization. Di-domain ARO/CYCs can further be separated into two subclasses: "nonreducing" ARO/CYCs, which act on nonreduced poly-beta-ketones, and "reducing" ARO/CYCs, which act on cyclized C9 reduced poly-beta-ketones. For years, the functional role of each domain in cyclization and aromatization for di-domain ARO/CYCs has remained a mystery. Here we present what is to our knowledge the first structural and functional analysis, along with an in-depth comparison, of the nonreducing (StfQ) and reducing (BexL) di-domain ARO/CYCs. This work completes the structural and functional characterization of mono- and di-domain ARO/CYCs in bacterial type II polyketide synthases and lays the groundwork for engineered biosynthesis of new bioactive polyketides. | ||
| - | |||
| - | Structural and functional analysis of two di-domain aromatase/cyclases from type II polyketide synthases.,Caldara-Festin G, Jackson DR, Barajas JF, Valentic TR, Patel AB, Aguilar S, Nguyen M, Vo M, Khanna A, Sasaki E, Liu HW, Tsai SC Proc Natl Acad Sci U S A. 2015 Dec 2. pii: 201512976. PMID:26631750<ref>PMID:26631750</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4xrt" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of the di-domain ARO/CYC StfQ from the steffimycin biosynthetic pathway
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Categories: Large Structures | Streptomyces steffisburgensis | Aguilar S | Barajas JF | Caldara-Festin GM | Jackson DR | Khanna A | Liu H-W | Nguyen M | Patel A | Sasaki E | Tsai SC | Valentic TR | Vo M
