PDBsum entry 2zc0

Transferase

PDB id: 2zc0

Contents

Protein chains

405 a.a. *

Ligands

PMP ×4

IMD ×4

Metals

_ZN ×4

Waters ×382

* Residue conservation analysis

PDB id:

2zc0

Name:

Transferase

Title:

Crystal structure of an archaeal alanine:glyoxylate aminotransferase

Structure:

Alanine glyoxylate transaminase. Chain: a, b, c, d. Synonym: alanine:glyoxylate aminotransferase. Engineered: yes

Source:

Thermococcus litoralis. Organism_taxid: 2265. Strain: dsm5473. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.30Å R-factor: 0.236 R-free: 0.261

Authors:

H.Sakuraba,K.Yoneda,H.Tsuge,T.Ohshima

Key ref:

H.Sakuraba et al. (2008). Structure of an archaeal alanine:glyoxylate aminotransferase. Acta Crystallogr D Biol Crystallogr, 64, 696-699. PubMed id: 18560158 DOI: 10.1107/S0907444908006732

Date:

31-Oct-07 Release date: 17-Jun-08

Protein chains

Q9C4M4  (Q9C4M4_THELI) -  Alanine glyoxylate transaminase from Thermococcus litoralis

Seq: 407 a.a.

Struc: 405 a.a.

Enzyme reactions

• Enzyme class: E.C.2.6.1.44 - alanine--glyoxylate transaminase.
• Reaction: glyoxylate + L-alanine = glycine + pyruvate

glyoxylate + L-alanine = glycine (Bound ligand (Het Group name = IMD) matches with 42.86% similarity) + pyruvate

• Cofactor: Pyridoxal 5'-phosphate

Pyridoxal 5'-phosphate (Bound ligand (Het Group name = PMP) matches with 88.24% similarity)

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

reference

DOI no: 10.1107/S0907444908006732

Acta Crystallogr D Biol Crystallogr 64:696-699 (2008)

PubMed id: 18560158

Structure of an archaeal alanine:glyoxylate aminotransferase.

H.Sakuraba, K.Yoneda, K.Takeuchi, H.Tsuge, N.Katunuma, T.Ohshima.

ABSTRACT

The crystal structure of a novel alanine:glyoxylate aminotransferase from the hyperthermophilic archaeon Thermococcus litoralis was determined at 2.3 A resolution. The asymmetric unit contains four homologous subunits and the functional tetramer is generated by noncrystallographic 222 symmetry. Although the main-chain coordinates of the monomer of the Thermococcus litoralis enzyme showed a high degree of similarity to those of aspartate aminotransferase from Thermus thermophilus HB8, the amino-acid residues involved in substrate binding in the aspartate aminotransferase are only partially conserved in the Thermococcus litoralis enzyme. This may account for the difference in the substrate specificities of the two enzymes.

Selected figure(s)

Figure 2.
Figure 2 Stereographic close-up of the substrate-binding site. The structure of Tc. litoralis AGT (green) is superimposed on that of Tm. thermophilus AspAT (yellow). The maleate molecule is shown as a stick model in cyan. The putative interactions are shown by dotted lines. N and O atoms are shown in blue and red, respectively.

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2008, 64, 696-699) copyright 2008.

Figure was selected by an automated process.