PDBsum entry 1vjo

Transferase

PDB id: 1vjo

Contents

Protein chain

377 a.a. *

Ligands

PLP

Waters ×432

* Residue conservation analysis

PDB id:

1vjo

Name:

Transferase

Title:

Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution

Structure:

Alanine--glyoxylate aminotransferase. Chain: a. Engineered: yes

Source:

Nostoc sp.. Organism_taxid: 103690. Strain: pcc 7120. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PDB file)

Resolution:

1.70Å R-factor: 0.154 R-free: 0.202

Authors:

Joint Center For Structural Genomics (Jcsg)

Key ref:

G.W.Han et al. (2005). Crystal structure of an alanine-glyoxylate aminotransferase from Anabaena sp. at 1.70 A resolution reveals a noncovalently linked PLP cofactor. Proteins, 58, 971-975. PubMed id: 15657930 DOI: 10.1002/prot.20360

Date:

16-Mar-04 Release date: 23-Mar-04

Protein chain

Q8YY48  (Q8YY48_NOSS1) -  Alanine--glyoxylate aminotransferase from Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)

Seq: 381 a.a.

Struc: 377 a.a.

Enzyme reactions

• Enzyme class: E.C.2.6.1.44 - alanine--glyoxylate transaminase.
• Reaction: glyoxylate + L-alanine = glycine + pyruvate
• Cofactor: Pyridoxal 5'-phosphate

Pyridoxal 5'-phosphate (Bound ligand (Het Group name = PLP) corresponds exactly)

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

reference

DOI no: 10.1002/prot.20360

Proteins 58:971-975 (2005)

PubMed id: 15657930

Crystal structure of an alanine-glyoxylate aminotransferase from Anabaena sp. at 1.70 A resolution reveals a noncovalently linked PLP cofactor.

G.W.Han, R.Schwarzenbacher, R.Page, L.Jaroszewski, P.Abdubek, E.Ambing, T.Biorac, J.M.Canaves, H.J.Chiu, X.Dai, A.M.Deacon, M.DiDonato, M.A.Elsliger, A.Godzik, C.Grittini, S.K.Grzechnik, J.Hale, E.Hampton, J.Haugen, M.Hornsby, H.E.Klock, E.Koesema, A.Kreusch, P.Kuhn, S.A.Lesley, I.Levin, D.McMullan, T.M.McPhillips, M.D.Miller, A.Morse, K.Moy, E.Nigoghossian, J.Ouyang, J.Paulsen, K.Quijano, R.Reyes, E.Sims, G.Spraggon, R.C.Stevens, H.van den Bedem, J.Velasquez, J.Vincent, F.von Delft, X.Wang, B.West, A.White, G.Wolf, Q.Xu, O.Zagnitko, K.O.Hodgson, J.Wooley, I.A.Wilson.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 1.
Figure 1. Crystal structure of AGT from Anabaena sp. (A) Stereo ribbon diagram of Anabena sp. AGT color-coded from N-terminus (blue) to C-terminus (red), showing the domain organization and location of the putative active site (PLP molecule shown in ball-and-stick representation). Helices H1-H15 and -strands ( 1- 12), as well as -sheets A, B, and C are indicated. (B) Diagram showing the secondary structure elements in Anabaena sp. AGT superimposed on its primary sequence. The -sheet designations are indicated by a red A, B, and C. Above each -strand, -bulges and -turns are indicated. -hairpins are depicted as red loops. Disordered regions are depicted by a dashed line, with the corresponding sequence in brackets.

Figure 2.
Figure 2. (A) Ribbon diagram of the Anabaena sp. AGT dimer. The N-terminal segment (red), N-terminal domain (green), and C-terminal domain (blue) are indicated for chain A. (B) Superposition of Anabaena sp. AGT (blue) and human AGT (PDB code: 1h0c; gray). The corresponding bound PLP and LLP (lysine-pyridoxal-5 -phosphate) ligands are shown in ball-and-stick representation, and regions of structural difference are labeled. (C) The PLP molecule bound to the active site of Anabaena sp. AGT and interacting residues are shown in ball-and-stick representation. 2Fo-Fc density for PLP contoured at 1 is shown in blue. (D) Superposition of the active sites with the PLP and LLP molecules and interacting residues from Anabaena sp. AGT (blue) and their counterparts in human AGT (gray, residues labeled in brackets) in ball-and-stick representation.

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 58, 971-975) copyright 2005.