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6iym
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Fumarylacetoacetate hydrolase (EaFAH) from psychrophilic Exiguobacterium antarcticum== | |
| + | <StructureSection load='6iym' size='340' side='right'caption='[[6iym]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6iym]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IYM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IYM FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6iym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iym OCA], [http://pdbe.org/6iym PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6iym RCSB], [http://www.ebi.ac.uk/pdbsum/6iym PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6iym ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fumarylacetoacetate hydrolase (FAH) is essential for the degradation of aromatic amino acids as well as for the cleavage of carbon-carbon bonds in metabolites or small organic compounds. Here, the X-ray crystal structure of EaFAH, a dimeric fumarylacetoacetate hydrolase from Exiguobacterium antarcticum, was determined, and its functional properties were investigated using biochemical methods. EaFAH adopts a mixed beta-sandwich roll fold with a highly flexible lid region (Val(73)-Leu(94)), and an Mg(2+) ion is bound at the active site by coordinating to the three carboxylate oxygen atoms of Glu(124), Glu(126), and Asp(155). The hydrolytic activity of EaFAH toward various substrates, including linalyl acetate was investigated using native polyacrylamide gel electrophoresis, activity staining, gel filtration, circular dichroism spectroscopy, fluorescence, and enzyme assays. | ||
| - | + | Structural and functional analysis of a dimeric fumarylacetoacetate hydrolase (EaFAH) from psychrophilic Exiguobacterium antarcticum.,Yoo W, Lee CW, Kim BY, Huong Luu Le LT, Park SH, Kim HW, Shin SC, Kim KK, Lee JH, Kim TD Biochem Biophys Res Commun. 2019 Feb 12;509(3):773-778. doi:, 10.1016/j.bbrc.2018.12.183. Epub 2019 Jan 8. PMID:30630595<ref>PMID:30630595</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Lee, | + | <div class="pdbe-citations 6iym" style="background-color:#fffaf0;"></div> |
| - | [[Category: Lee, | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lee, C W]] | ||
| + | [[Category: Lee, J H]] | ||
| + | [[Category: Exiguobacterium antarctica]] | ||
| + | [[Category: Fumarylacetoacetate hydrolase]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 07:03, 3 April 2019
Fumarylacetoacetate hydrolase (EaFAH) from psychrophilic Exiguobacterium antarcticum
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