PDBsum entry 1jal

Structural genomics, unknown function

PDB id: 1jal

Contents

Protein chains

348 a.a. *

Waters ×484

* Residue conservation analysis

PDB id:

1jal

Name:

Structural genomics, unknown function

Title:

Ychf protein (hi0393)

Structure:

Ychf protein. Chain: a, b. Synonym: hi0393, probable gtp-binding protein hi0393. Engineered: yes

Source:

Haemophilus influenzae. Organism_taxid: 727. Gene: ychf. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.40Å R-factor: 0.208 R-free: 0.247

Authors:

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

Key ref:

A.Teplyakov et al. (2003). Crystal structure of the YchF protein reveals binding sites for GTP and nucleic acid. J Bacteriol, 185, 4031-4037. PubMed id: 12837776

Date:

30-May-01 Release date: 25-Mar-03

Protein chains

P44681  (YCHF_HAEIN) -  Ribosome-binding ATPase YchF from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Seq: 363 a.a.

Struc: 348 a.a.

Enzyme reactions

• Enzyme class: E.C.?

J Bacteriol 185:4031-4037 (2003)

PubMed id: 12837776

Crystal structure of the YchF protein reveals binding sites for GTP and nucleic acid.

A.Teplyakov, G.Obmolova, S.Y.Chu, J.Toedt, E.Eisenstein, A.J.Howard, G.L.Gilliland.

ABSTRACT

The bacterial protein encoded by the gene ychF is 1 of 11 universally conserved GTPases and the only one whose function is unknown. The crystal structure determination of YchF was sought to help with the functional assignment of the protein. The YchF protein from Haemophilus influenzae was cloned and expressed, and the crystal structure was determined at 2.4 A resolution. The polypeptide chain is folded into three domains. The N-terminal domain has a mononucleotide binding fold typical for the P-loop NTPases. An 80-residue domain next to it has a pronounced alpha-helical coiled coil. The C-terminal domain features a six-stranded half-barrel that curves around an alpha-helix. The crablike three-domain structure of YchF suggests the binding site for a double-stranded nucleic acid in the cleft between the domains. The structure of the putative GTP-binding site is consistent with the postulated guanine specificity of the protein. Fluorescence measurements have demonstrated the ability of YchF to bind a double-stranded nucleic acid and GTP. Taken together with other experimental data and genomic analysis, these results suggest that YchF may be part of a nucleoprotein complex and may function as a GTP-dependent translation factor.