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4W5K

Structure of a mitochondrial aspartate aminotransferase from Trypanosoma brucei, K237A mutant

Summary for 4W5K
Entry DOI10.2210/pdb4w5k/pdb
Related4EU1
DescriptorAspartate aminotransferase, mitochondrial, PYRIDOXAL-5'-PHOSPHATE, D-MALATE, ... (5 entities in total)
Functional Keywordsssgcid, aspartate aminotransferase, mitochondrial, trypanosoma brucei, structural genomics, seattle structural genomics center for infectious disease, transferase
Biological sourceTrypanosoma brucei brucei
Total number of polymer chains2
Total formula weight88524.85
Authors
Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2014-08-18, release date: 2014-09-24, Last modification date: 2024-12-25)
Primary citationAbendroth, 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.,Sect.F, 71:566-571, 2015
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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数据于2025-10-22公开中

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