5wyf
From Proteopedia
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<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=5wyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wyf OCA], [http://pdbe.org/5wyf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wyf RCSB], [http://www.ebi.ac.uk/pdbsum/5wyf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wyf 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=5wyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wyf OCA], [http://pdbe.org/5wyf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wyf RCSB], [http://www.ebi.ac.uk/pdbsum/5wyf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wyf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Crystal structures of Lactobacillus buchneri isoleucine 2-epimerase, a novel branched-chain amino-acid racemase, were determined for the enzyme in the apo form, in complex with pyridoxal 5'-phosphate (PLP), in complex with N-(5'-phosphopyridoxyl)-L-isoleucine (PLP-L-Ile) and in complex with N-(5'-phosphopyridoxyl)-D-allo-isoleucine (PLP-D-allo-Ile) at resolutions of 2.77, 1.94, 2.65 and 2.12 A, respectively. The enzyme assembled as a tetramer, with each subunit being composed of N-terminal, C-terminal and large PLP-binding domains. The active-site cavity in the apo structure was much more solvent-accessible than that in the PLP-bound structure. This indicates that a marked structural change occurs around the active site upon binding of PLP that provides a solvent-inaccessible environment for the enzymatic reaction. The main-chain coordinates of the L. buchneri isoleucine 2-epimerase monomer showed a notable similarity to those of alpha-amino--caprolactam racemase from Achromobactor obae and gamma-aminobutyrate aminotransferase from Escherichia coli. However, the amino-acid residues involved in substrate binding in those two enzymes are only partially conserved in L. buchneri isoleucine 2-epimerase, which may account for the differences in substrate recognition by the three enzymes. The structures bound with reaction-intermediate analogues (PLP-L-Ile and PLP-D-allo-Ile) and site-directed mutagenesis suggest that L-isoleucine epimerization proceeds through abstraction of the alpha-hydrogen of the substrate by Lys280, while Asp222 serves as the catalytic residue adding an alpha-hydrogen to the quinonoid intermediate to form D-allo-isoleucine. | ||
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| + | Crystal structure of the novel amino-acid racemase isoleucine 2-epimerase from Lactobacillus buchneri.,Hayashi J, Mutaguchi Y, Minemura Y, Nakagawa N, Yoneda K, Ohmori T, Ohshima T, Sakuraba H Acta Crystallogr D Struct Biol. 2017 May 1;73(Pt 5):428-437. doi:, 10.1107/S2059798317005332. Epub 2017 Apr 19. PMID:28471367<ref>PMID:28471367</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5wyf" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 09:07, 17 May 2017
Structure of amino acid racemase, 2.12 A
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