PDBsum entry 1fl9

Structural genomics, unknown function

PDB id: 1fl9

Contents

Protein chains

157 a.a. *

Metals

_HG ×3

Waters ×31

* Residue conservation analysis

PDB id:

1fl9

Name:

Structural genomics, unknown function

Title:

The yjee protein

Structure:

Hypothetical protein hi0065. Chain: a, b, c. Engineered: yes

Source:

Haemophilus influenzae. Organism_taxid: 727. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.50Å R-factor: 0.220 R-free: 0.285

Authors:

A.Teplyakov,G.L.Gilliland,Structure 2 Function Project (S2f)

Key ref:

A.Teplyakov et al. (2002). Crystal structure of the YjeE protein from Haemophilus influenzae: a putative Atpase involved in cell wall synthesis. Proteins, 48, 220-226. PubMed id: 12112691 DOI: 10.1002/prot.10114

Date:

13-Aug-00 Release date: 07-Aug-02

Protein chains

P44492  (TSAE_HAEIN) -  tRNA threonylcarbamoyladenosine biosynthesis protein TsaE from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Seq: 158 a.a.

Struc: 157 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1002/prot.10114

Proteins 48:220-226 (2002)

PubMed id: 12112691

Crystal structure of the YjeE protein from Haemophilus influenzae: a putative Atpase involved in cell wall synthesis.

A.Teplyakov, G.Obmolova, M.Tordova, N.Thanki, N.Bonander, E.Eisenstein, A.J.Howard, G.L.Gilliland.

ABSTRACT

A hypothetical protein encoded by the gene YjeE of Haemophilus influenzae was selected as part of a structural genomics project for X-ray analysis to assist with the functional assignment. The protein is considered essential to bacteria because the gene is present in virtually all bacterial genomes but not in those of archaea or eukaryotes. The amino acid sequence shows no homology to other proteins except for the presence of the Walker A motif G-X-X-X-X-G-K-T that indicates the possibility of a nucleotide-binding protein. The YjeE protein was cloned, expressed, and the crystal structure determined by the MAD method at 1.7-A resolution. The protein has a nucleotide-binding fold with a four-stranded parallel beta-sheet flanked by antiparallel beta-strands on each side. The topology of the beta-sheet is unique among P-loop proteins and has features of different families of enzymes. Crystallization of YjeE in the presence of ATP and Mg2+ resulted in the structure with ADP bound in the P-loop. The ATPase activity of YjeE was confirmed by kinetic measurements. The distribution of conserved residues suggests that the protein may work as a "molecular switch" triggered by ATP hydrolysis. The phylogenetic pattern of YjeE suggests its involvement in cell wall biosynthesis.

Selected figure(s)

Figure 1.
Figure 1. Ribbon presentation of the polypeptide fold of YjeE. Conserved amino acids and ADP-Mg^2+ are shown as ball- and-stick models.

Figure 3.
Figure 3. Stereo view of the (2F[o]-F[c]) electron density map at the nucleotide site in monomer A. The map is contoured at the 2 level. ADP atoms and Mg^2+ were omitted for phase calculation. The final model for ADP, Mg^2+, and its three water ligands is shown.

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2002, 48, 220-226) copyright 2002.

Figures were selected by an automated process.