4xrt

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<StructureSection load='4xrt' size='340' side='right'caption='[[4xrt]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='4xrt' size='340' side='right'caption='[[4xrt]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4xrt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_steffisburgensis"_dietz "streptomyces steffisburgensis" dietz]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XRT FirstGlance]. <br>
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<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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.952&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tfz|3tfz]], [[2rer|2rer]], [[2rez|2rez]], [[2kf2|2kf2]], [[4xrw|4xrw]]</td></tr>
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<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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">stfQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=68271 "Streptomyces steffisburgensis" Dietz])</td></tr>
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<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>
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<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=4xrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xrt OCA], [http://pdbe.org/4xrt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xrt RCSB], [http://www.ebi.ac.uk/pdbsum/4xrt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xrt ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q2PA00_9ACTN Q2PA00_9ACTN]
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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.
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4xrt" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Streptomyces steffisburgensis dietz]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Aguilar, S]]
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[[Category: Streptomyces steffisburgensis]]
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[[Category: Barajas, J F]]
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[[Category: Aguilar S]]
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[[Category: Caldara-Festin, G M]]
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[[Category: Barajas JF]]
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[[Category: Jackson, D R]]
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[[Category: Caldara-Festin GM]]
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[[Category: Khanna, A]]
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[[Category: Jackson DR]]
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[[Category: Liu, H W]]
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[[Category: Khanna A]]
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[[Category: Nguyen, M]]
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[[Category: Liu H-W]]
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[[Category: Patel, A]]
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[[Category: Nguyen M]]
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[[Category: Sasaki, E]]
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[[Category: Patel A]]
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[[Category: Tsai, S C]]
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[[Category: Sasaki E]]
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[[Category: Valentic, T R]]
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[[Category: Tsai SC]]
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[[Category: Vo, M]]
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[[Category: Valentic TR]]
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[[Category: Aro/cyc]]
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[[Category: Vo M]]
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[[Category: Aromatase/cyclase]]
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[[Category: Dehydratase]]
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[[Category: Helix-grip fold]]
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[[Category: Lyase]]
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[[Category: Natural product]]
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[[Category: Polyketide]]
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[[Category: Polyketide synthase]]
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Current revision

Crystal structure of the di-domain ARO/CYC StfQ from the steffimycin biosynthetic pathway

PDB ID 4xrt

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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