PDBsum entry 4ix8

Transferase

PDB id: 4ix8

Contents

Protein chains

407 a.a.

370 a.a.

Metals

_CL ×2

Waters ×274

PDB id:

4ix8

Name:

Transferase

Title:

Crystal structure of tyrosine aminotransferase from leishmania infantum

Structure:

Tyrosine aminotransferase. Chain: a, b. Fragment: leina.00674.A.Bv2. Engineered: yes

Source:

Leishmania infantum. Organism_taxid: 5671. Gene: linj_36_2490, tat. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.35Å R-factor: 0.175 R-free: 0.206

Authors:

Seattle Structural Genomics Center For Infectious Disease (Ssgcid)

Key ref:

M.A.Moreno et al. (2014). Structure of tyrosine aminotransferase from Leishmania infantum. Acta Crystallogr F Struct Biol Commun, 70, 583-587. PubMed id: 24817714 DOI: 10.1107/S2053230X14007845

Date:

24-Jan-13 Release date: 26-Mar-14

Protein chain

A4IDL0  (A4IDL0_LEIIN) -  Tyrosine aminotransferase from Leishmania infantum

Seq: 448 a.a.

Struc: 407 a.a.*

Protein chain

A4IDL0  (A4IDL0_LEIIN) -  Tyrosine aminotransferase from Leishmania infantum

Seq: 448 a.a.

Struc: 370 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B: E.C.2.6.1.5 - tyrosine transaminase.
• Pathway: Phenylalanine and Tyrosine Biosynthesis
• Reaction: L-tyrosine + 2-oxoglutarate = 3-(4-hydroxyphenyl)pyruvate + L-glutamate
• Cofactor: Pyridoxal 5'-phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1107/S2053230X14007845

Acta Crystallogr F Struct Biol Commun 70:583-587 (2014)

PubMed id: 24817714

Structure of tyrosine aminotransferase from Leishmania infantum.

M.A.Moreno, A.Abramov, J.Abendroth, A.Alonso, S.Zhang, P.J.Alcolea, T.Edwards, D.Lorimer, P.J.Myler, V.Larraga.

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.