PDBsum entry 2g0q

Structural genomics, unknown function

PDB id: 2g0q

Contents

Protein chain

149 a.a. *

* Residue conservation analysis

PDB id:

2g0q

Name:

Structural genomics, unknown function

Title:

Solution structure of at5g39720.1 from arabidopsis thaliana

Structure:

At5g39720.1 protein. Chain: a. Engineered: yes

Source:

Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Gene: at5g39720.1. Other_details: wheat germ cell-free, in vitro expression

NMR struc:

20 models

Authors:

B.F.Volkman,F.C.Peterson,B.L.Lytle,Center For Eukaryotic Structural Genomics (Cesg)

Key ref:

B.L.Lytle et al. (2006). Solution structure of Arabidopsis thaliana protein At5g39720.1, a member of the AIG2-like protein family. Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 490-493. PubMed id: 16754964 DOI: 10.1107/S1744309106015946

Date:

13-Feb-06 Release date: 28-Feb-06

Protein chain

Q9FIX2  (AIGLA_ARATH) -  AIG2-like protein A from Arabidopsis thaliana

Seq: 165 a.a.

Struc: 149 a.a.

Enzyme reactions

• Enzyme class: E.C.2.3.2.- - ?????

DOI no: 10.1107/S1744309106015946

Acta Crystallogr Sect F Struct Biol Cryst Commun 62:490-493 (2006)

PubMed id: 16754964

Solution structure of Arabidopsis thaliana protein At5g39720.1, a member of the AIG2-like protein family.

B.L.Lytle, F.C.Peterson, E.M.Tyler, C.L.Newman, D.A.Vinarov, J.L.Markley, B.F.Volkman.

ABSTRACT

The three-dimensional structure of Arabidopsis thaliana protein At5g39720.1 was determined by NMR spectroscopy. It is the first representative structure of Pfam family PF06094, which contains protein sequences similar to that of AIG2, an A. thaliana protein of unknown function induced upon infection by the bacterial pathogen Pseudomonas syringae. The At5g39720.1 structure consists of a five-stranded beta-barrel surrounded by two alpha-helices and a small beta-sheet. A long flexible alpha-helix protrudes from the structure at the C-terminal end. A structural homology search revealed similarity to three members of Pfam family UPF0131. Conservation of residues in a hydrophilic cavity able to bind small ligands in UPF0131 proteins suggests that this may also serve as an active site in AIG2-like proteins.

Selected figure(s)

Figure 1.
NMR data and structure of At5g39720.1. (a) Two-dimensional ^1H --^15N HSQC spectrum for (U-^13C,^15N) At5g39720.1 acquired at 298 K and 600 MHz. (b) Ribbon diagram of a representative conformer in stereoview. Residues of the N-terminal tag (1 --9) and the disordered C-terminus (159 --173) are omitted for clarity and were not included in the coordinates deposited in the PDB. (c) Ensemble of 20 conformers shown as a C^[alpha] trace in the same orientation as in (b) (left) and rotated 90[deg] about the horizontal axis (right). (d) Backbone (N, C^[alpha], C[prime prime or minute]) r.m.s.d. values and (e) ^1H --^15N heteronuclear NOEs plotted for each residue of At5g39720.1. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 June 1; 62(Pt 6): 490–493. Published online 2006 May 31. doi: 10.1107/S1744309106015946. Copyright [copyright] International Union of Crystallography 2006

Figure 2.
At5g39720.1 and its structural homologs. (a) Ribbon diagrams of At5g39720.1, E. coli YtfP (PDB code 1xhs), Pyrococcus horikoshii PH0828 (PDB code 1v30) and murine 13879369 (PDB code 1vkb). (b) Multiple sequence alignment of the At5g39720.1 homologs shown in (a) and representative members of the AIG2-like family (identified by species and SWISS-PROT ID) from a plant (Oryza sativa Q6Z2W4), fungi (Yarrowia lipolytica Q6CD06 and Neuropora crassa Q9HEJ2) and a bacterium (Frankia sp. CcI3 Q2JFJ8). The residue numbering corresponds to the actual At5g39720.1 sequence without N-terminal His tag and thus differs by eight from the PDB numbering shown in Fig. 1 [triangle] Figure 1-(a). Residues identical in at least seven of eight sequences are shaded red and highly conserved residues are colored blue. Conserved residues lining the cavity are highlighted in orange. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 June 1; 62(Pt 6): 490–493. Published online 2006 May 31. doi: 10.1107/S1744309106015946. Copyright [copyright] International Union of Crystallography 2006

The above figures are reprinted from an Open Access publication published by the IUCr: Acta Crystallogr Sect F Struct Biol Cryst Commun (2006, 62, 490-493) copyright 2006.