6jvv
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of maleylpyruvate hydrolase from Sphingobium.sp SYK-6== | |
| + | <StructureSection load='6jvv' size='340' side='right'caption='[[6jvv]], [[Resolution|resolution]] 1.51Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6jvv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JVV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JVV FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6jvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jvv OCA], [http://pdbe.org/6jvv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jvv RCSB], [http://www.ebi.ac.uk/pdbsum/6jvv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jvv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Sphingobium sp. strain SYK-6, an aerobic gram-negative bacillus found in soil, is known for utilizing lignin-derived monoaryls and biaryls as carbon sources and degrading aromatic compounds. The Sphingobium sp. strain SYK-6 genome contains three genes involved in salicylate catabolism: SLG_11260, SLG_11270, and SLG_11280. Here, we report that the gene product of SLG_11280 functions as a maleylpyruvate hydrolase (SsMPH) with Km and Kcat values of 166.2muM and 3.76 min(-1), respectively. This study also reveals the crystal structures of both the apo and pyruvate-manganese ion-bound SsMPH, which revealed that like other fumarylacetoacetate hydrolases, SsMPH dimerizes and has nine unique 310-helices. Molecular docking studies of maleylpyruvate also revealed the likely binding mode of SsMPH and its substrate. | ||
| - | + | Structural insights into a maleylpyruvate hydrolase from sphingobium sp. SYK-6, a bacterium degrading lignin-derived aryls.,Hong H, Seo H, Kim KJ Biochem Biophys Res Commun. 2019 May 9. pii: S0006-291X(19)30898-8. doi:, 10.1016/j.bbrc.2019.05.030. PMID:31079929<ref>PMID:31079929</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 6jvv" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Hong, H]] | [[Category: Hong, H]] | ||
| + | [[Category: Kim, K J]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 06:12, 29 May 2019
Crystal structure of maleylpyruvate hydrolase from Sphingobium.sp SYK-6
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