6jvw: Difference between revisions
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==Crystal structure of maleylpyruvate hydrolase from Sphingobium sp. SYK-6 in complex with manganese (II) ion and pyruvate== | |||
<StructureSection load='6jvw' size='340' side='right'caption='[[6jvw]], [[Resolution|resolution]] 2.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6jvw]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JVW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JVW 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=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</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=6jvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jvw OCA], [http://pdbe.org/6jvw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jvw RCSB], [http://www.ebi.ac.uk/pdbsum/6jvw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jvw 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> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6jvw" 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 in complex with manganese (II) ion and pyruvate
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