5xgv
From Proteopedia
(Difference between revisions)
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==The structure of Diels-Alderase PyrE3 in the biosynthetic pathway of pyrroindomycins== | ==The structure of Diels-Alderase PyrE3 in the biosynthetic pathway of pyrroindomycins== | ||
| - | <StructureSection load='5xgv' size='340' side='right' caption='[[5xgv]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='5xgv' size='340' side='right'caption='[[5xgv]], [[Resolution|resolution]] 2.10Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5xgv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XGV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XGV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xgv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/'streptomyces_rugosporus' 'streptomyces rugosporus']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XGV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XGV FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pyrE3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=295838 'Streptomyces rugosporus'])</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=5xgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xgv OCA], [http://pdbe.org/5xgv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xgv RCSB], [http://www.ebi.ac.uk/pdbsum/5xgv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xgv ProSAT]</span></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=5xgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xgv OCA], [http://pdbe.org/5xgv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xgv RCSB], [http://www.ebi.ac.uk/pdbsum/5xgv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xgv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Here, we provide structural insights into PyrE3, a flavin-dependent [4 + 2] cyclase that catalyzes trans-decalin formation in the biosynthesis of pyrroindomycins. PyrE3 shares an architecture/domain organization head-to-tail similarity with the members of the family of para-hydroxybenzoate hydroxylase (pHBH)-fold monooxygenases, and possesses a flavin adenine dinucleotide (FAD)-binding domain, a middle domain, and a C-terminal thioredoxin-like domain. The FAD-binding domain forms a central hub of the protein structure, and binds with FAD in a "closed" conformation of pHBH-fold family monooxygenases known for their highly dynamic catalytic processes. FAD plays an essential structural role in PyrE3, where it is amenable to redox change; however, redox change has little effect on [4 + 2] cyclization activity. PyrE3 appears to selectively accommodate a tetramate-containing, linear polyene intermediate in a highly positively charged pocket, which is located at the interface between the FAD-binding domain and the middle domain, and can accelerate trans-decalin formation likely through an endo-selective [4 + 2] transition state. | ||
| + | |||
| + | Structural Insights into a Flavin-Dependent [4 + 2] Cyclase that Catalyzes trans-Decalin Formation in Pyrroindomycin Biosynthesis.,Zheng Q, Gong Y, Guo Y, Zhao Z, Wu Z, Zhou Z, Chen D, Pan L, Liu W Cell Chem Biol. 2018 Jun 21;25(6):718-727.e3. doi:, 10.1016/j.chembiol.2018.03.007. Epub 2018 Apr 12. PMID:29657086<ref>PMID:29657086</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5xgv" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Streptomyces rugosporus]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Gong, Y]] | [[Category: Gong, Y]] | ||
[[Category: Guo, Y]] | [[Category: Guo, Y]] | ||
Revision as of 08:06, 21 May 2019
The structure of Diels-Alderase PyrE3 in the biosynthetic pathway of pyrroindomycins
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