4H51

Crystal structure of a putative Aspartate Aminotransferase from Leishmania major Friedlin

Summary for 4H51

• Entry DOI: 10.2210/pdb4h51/pdb
• Descriptor: Aspartate aminotransferase, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: ssgcid, leishmania major, structural genomics, seattle structural genomics center for infectious disease, aspartate aminotransferase, transferase, pyridoxal phosphate
• Biological source: Leishmania major
• Total number of polymer chains: 2
• Total formula weight: 94727.46

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2012-09-18, release date: 2012-10-10, Last modification date: 2025-03-26)

Primary citation

Abendroth, J.,Choi, R.,Wall, A.,Clifton, M.C.,Lukacs, C.M.,Staker, B.L.,Van Voorhis, W.,Myler, P.,Lorimer, D.D.,Edwards, T.E.
Structures of aspartate aminotransferases from Trypanosoma brucei, Leishmania major and Giardia lamblia.
Acta Crystallogr F Struct Biol Commun, 71:566-571, 2015

PubMed 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.

PubMed: 25945710
DOI: 10.1107/S2053230X15001831

Experimental method

X-RAY DIFFRACTION (1.85 Å)