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Acta Crystallogr F Struct Biol Commun. 2015 May;71(Pt 5):566-71. doi: 10.1107/S2053230X15001831. Epub 2015 Apr 21.

Structures of aspartate aminotransferases from Trypanosoma brucei, Leishmania major and Giardia lamblia.

Author information

1
Seattle Structural Genomics Center for Infectious Disease, http://www.ssgcid.org, USA.

Abstract

The structures of three aspartate aminotransferases (AATs) from eukaryotic pathogens were solved within the Seattle Structural Genomics Center for Infectious Disease (SSGCID). Both the open and closed conformations of AAT were observed. Pyridoxal phosphate was bound to the active site via a Schiff base to a conserved lysine. An active-site mutant showed that Trypanosoma brucei AAT still binds pyridoxal phosphate even in the absence of the tethering lysine. The structures highlight the challenges for the structure-based design of inhibitors targeting the active site, while showing options for inhibitor design targeting the N-terminal arm.

KEYWORDS:

Giardia lamblia; Leishmania major; Seattle Structural Genomics Center for Infectious Disease; Trypanosoma brucei; aspartate aminotransferase; pyridoxalphosphate lysine; structural genomics; transferase

PMID:
25945710
PMCID:
PMC4427166
DOI:
10.1107/S2053230X15001831
[Indexed for MEDLINE]
Free PMC Article

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