Structural diversity in the six-fold redundant set of acyl-CoA carboxyltransferases in Mycobacterium tuberculosis

FEBS Letters

Volumn 580, Issue 30, 2006, Pages 6898-6902

  Holton, Simon J ^a   King Scott, Stephanie ^a   Eddine, Ali Nasser ^b   Kaufmann, Stefan H E ^b   Wilmanns, Matthias ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b MAX PLANCK INSTITUTE FOR INFECTION BIOLOGY   (Germany)

Author keywords

Acyl CoA carboxylase; Mycobaceterium tuberculosis; Protein complex reconstitution; Structural proteomics; X ray crystallography

Indexed keywords

CARBOXYLTRANSFERASE; PALMITOYL COENZYME A HYDROLASE;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME STRUCTURE; MOLECULAR DYNAMICS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; SURFACE PROPERTY;

ACYL COENZYME A; BINDING SITES; CARBOXYL AND CARBAMOYL TRANSFERASES; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; MYCOBACTERIUM TUBERCULOSIS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS;

MYCOBACTERIUM TUBERCULOSIS;

EID: 33845415806     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.11.054     Document Type: Article

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