High-resolution structures reveal details of domain closure and "half-of-sites-reactivity" in Escherichia coli aspartate β-semialdehyde dehydrogenase

Journal of Molecular Biology

Volumn 341, Issue 3, 2004, Pages 797-806

  Nichols, C E ^a   Dhaliwal, B ^a   Lockyer, M ^b   Hawkins, A R ^c   Stammers, D K ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b Arrow Therapeutics   (United Kingdom)

^c NEWCASTLE UNIVERSITY   (United Kingdom)

Author keywords

ASADH; ASADH, aspartate semialdehyde dehydrogenase; aspartate semialdehyde dehydrogenase; conformational changes; domain closure; half of sites reactivity; HOSR, half of sites reactivity; TAD, torsion angle difference plot

Indexed keywords

ASPARTATE SEMIALDEHYDE DEHYDROGENASE; PROTEIN SUBUNIT;

ARTICLE; BIOSYNTHESIS; DATA ANALYSIS; ENERGY; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; REACTION ANALYSIS; STRUCTURE ANALYSIS;

ESCHERICHIA COLI;

EID: 4344686148     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.05.073     Document Type: Article

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