4IX8

Crystal structure of Tyrosine aminotransferase from Leishmania infantum

4IX8 の概要

• エントリーDOI: 10.2210/pdb4ix8/pdb
• 分子名称: Tyrosine aminotransferase, CHLORIDE ION (3 entities in total)
• 機能のキーワード: ssgcid, tyrosine aminotransferase, pyridoxal phosphate, seattle structural genomics center for infectious disease, transferase
• 由来する生物種: Leishmania infantum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 99968.12

構造登録者

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2013-01-24, 公開日: 2014-03-26, 最終更新日: 2023-11-15)

主引用文献

Moreno, M.A.,Abramov, A.,Abendroth, J.,Alonso, A.,Zhang, S.,Alcolea, P.J.,Edwards, T.,Lorimer, D.,Myler, P.J.,Larraga, V.
Structure of tyrosine aminotransferase from Leishmania infantum.
Acta Crystallogr F Struct Biol Commun, 70:583-587, 2014

PubMed Abstract: The trypanosomatid parasite Leishmania infantum is the causative agent of visceral leishmaniasis (VL), which is usually fatal unless treated. VL has an incidence of 0.5 million cases every year and is an important opportunistic co-infection in HIV/AIDS. Tyrosine aminotransferase (TAT) has an important role in the metabolism of trypanosomatids, catalyzing the first step in the degradation pathway of aromatic amino acids, which are ultimately converted into their corresponding L-2-oxoacids. Unlike the enzyme in Trypanosoma cruzi and mammals, L. infantum TAT (LiTAT) is not able to transaminate ketoglutarate. Here, the structure of LiTAT at 2.35 Å resolution is reported, and it is confirmed that the presence of two Leishmania-specific residues (Gln55 and Asn58) explains, at least in part, this specific reactivity. The difference in substrate specificity between leishmanial and mammalian TAT and the importance of this enzyme in parasite metabolism suggest that it may be a useful target in the development of new drugs against leishmaniasis.

PubMed: 24817714
DOI: 10.1107/S2053230X14007845

実験手法

X-RAY DIFFRACTION (2.35 Å)