The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance

Acta Crystallographica Section D: Biological Crystallography

Volumn 61, Issue 8, 2005, Pages 1116-1124

  Dobson, Renwick C J ^a   Griffin, Michael D W ^a   Jameson, Geoffrey B ^b   Gerrard, Juliet A ^a  

^a UNIVERSITY OF CANTERBURY   (New Zealand)

^b MASSEY UNIVERSITY   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI;

DIHYDRODIPICOLINATE SYNTHASE; HYDROLYASE; LYSINE;

ARTICLE; BINDING SITE; CHEMISTRY; ENZYMOLOGY; ESCHERICHIA COLI; METHODOLOGY; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

ALLOSTERIC SITE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HYDRO-LYASES; LYSINE; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY;

EID: 25144446271     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444905016318     Document Type: Article

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