The narrow active-site cleft of O-acetylserine sulfhydrylase from Leishmania donovani allows complex formation with serine acetyltransferases with a range of C-terminal sequences

Acta Crystallographica Section D: Biological Crystallography

Volumn 68, Issue 8, 2012, Pages 909-919

  Raj, Isha ^a   Kumar, Sudhir ^a   Gourinath, Samudrala ^a  

^a JAWAHARLAL NEHRU UNIVERSITY   (India)

Author keywords

cysteine synthase complex; cysteine biosynthetic pathway; inhibition; regulation; SAT C terminus mimicking peptides

Indexed keywords

CYSTEINE SYNTHASE; PEPTIDE; SERINE ACETYLTRANSFERASE;

ARTICLE; CHEMISTRY; CONFORMATION; CRYSTALLIZATION; DIMERIZATION; ENZYME ACTIVE SITE; ENZYMOLOGY; LEISHMANIA DONOVANI; METHODOLOGY; MOLECULAR CLONING; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SPECTROFLUOROMETRY; X RAY CRYSTALLOGRAPHY;

CATALYTIC DOMAIN; CLONING, MOLECULAR; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CYSTEINE SYNTHASE; DIMERIZATION; LEISHMANIA DONOVANI; MOLECULAR CONFORMATION; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SERINE O-ACETYLTRANSFERASE; SPECTROMETRY, FLUORESCENCE;

EID: 84864865811     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444912016459     Document Type: Article

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