7jqy
From Proteopedia
(Difference between revisions)
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==Crystal structure of Cfl1-D123S from Burkholderia cenocepacia== | ==Crystal structure of Cfl1-D123S from Burkholderia cenocepacia== | ||
| - | <StructureSection load='7jqy' size='340' side='right'caption='[[7jqy]]' scene=''> | + | <StructureSection load='7jqy' size='340' side='right'caption='[[7jqy]], [[Resolution|resolution]] 2.15Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JQY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7jqy]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Burcj Burcj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JQY FirstGlance]. <br> |
| - | </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=7jqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jqy OCA], [https://pdbe.org/7jqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jqy RCSB], [https://www.ebi.ac.uk/pdbsum/7jqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jqy ProSAT]</span></td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7jqx|7jqx]]</div></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BCAM1529 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216591 BURCJ])</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=7jqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jqy OCA], [https://pdbe.org/7jqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jqy RCSB], [https://www.ebi.ac.uk/pdbsum/7jqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jqy ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Epoxide hydrolases catalyze the conversion of epoxides to vicinal diols in a range of cellular processes such as signaling, detoxification, and virulence. These enzymes typically utilize a pair of tyrosine residues to orient the substrate epoxide ring in the active site and stabilize the hydrolysis intermediate. A new subclass of epoxide hydrolases that utilize a histidine in place of one of the tyrosines was established with the discovery of the CFTR Inhibitory Factor (Cif) from Pseudomonas aeruginosa. Although the presence of such Cif-like epoxide hydrolases was predicted in other opportunistic pathogens based on sequence analyses, only Cif and its homolog aCif from Acinetobacter nosocomialis have been characterized. Here we report the biochemical and structural characteristics of Cfl1 and Cfl2, two Cif-like epoxide hydrolases from Burkholderia cenocepacia. Cfl1 is able to hydrolyze xenobiotic as well as biological epoxides that might be encountered in the environment or during infection. In contrast, Cfl2 shows very low activity against a diverse set of epoxides. The crystal structures of the two proteins reveal quaternary structures that build on the well-known dimeric assembly of the alpha/beta hydrolase domain, but broaden our understanding of the structural diversity encoded in novel oligomer interfaces. Analysis of the interfaces reveals both similarities and key differences in sequence conservation between the two assemblies, and between the canonical dimer and the novel oligomer interfaces of each assembly. Finally, we discuss the effects of these higher-order assemblies on the intra-monomer flexibility of Cfl1 and Cfl2 and their possible roles in regulating enzymatic activity. | ||
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| + | Biochemical and structural characterization of two cif-like epoxide hydrolases from Burkholderia cenocepacia.,Taher NM, Hvorecny KL, Burke CM, Gilman MSA, Heussler GE, Adolf-Bryfogle J, Bahl CD, O'Toole GA, Madden DR Curr Res Struct Biol. 2021 Feb 21;3:72-84. doi: 10.1016/j.crstbi.2021.02.002., eCollection 2021. PMID:34235487<ref>PMID:34235487</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7jqy" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Burcj]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Madden | + | [[Category: Madden, D R]] |
| - | [[Category: Taher | + | [[Category: Taher, N M]] |
| + | [[Category: Alpha/beta hydrolase fold]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Octamer]] | ||
Revision as of 10:48, 28 July 2021
Crystal structure of Cfl1-D123S from Burkholderia cenocepacia
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