Crystal Structure and Putative Mechanism of 3-Methylitaconate-Δ-isomerase from Eubacterium barkeri

Journal of Molecular Biology

Volumn 391, Issue 3, 2009, Pages 609-620

  Velarde, Milko ^a   Macieira, Sofia ^a   Hilberg, Markus ^b   Bröker, Gerd ^b   Tu, Shang Min ^c   Golding, Bernard T ^c   Pierik, Antonio J ^b   Buckel, Wolfgang ^b,d   Messerschmidt, Albrecht ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b PHILIPPS UNIVERSITY MARBURG   (Germany)

^c NEWCASTLE UNIVERSITY   (United Kingdom)

^d MAX PLANCK INSTITUTE FOR TERRESTRIAL MICROBIOLOGY   (Germany)

Author keywords

DapF family fold; methylitaconate isomerase; open and closed conformations; PrpF protein; X ray structure

Indexed keywords

3 METHYLITACONATE DELTA ISOMERASE; BACTERIAL ENZYME; CYSTEINE; GLUTAMIC ACID; HISTIDINE; ISOMERASE; ISOPENTENYL DIPHOSPHATE DELTA ISOMERASE; LYSINE; SERINE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANAEROBIC BACTERIUM; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; EUBACTERIUM; EUBACTERIUM BARKERI; MOLECULAR CLONING; MOLECULAR DOCKING; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTON TRANSPORT; SOIL MICROFLORA; WILD TYPE; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS); CLOSTRIDIALES; ESCHERICHIA COLI; EUBACTERIUM BARKERI;

EID: 67651149462     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.06.052     Document Type: Article

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