Skip to main content
U.S. flag

An official website of the United States government

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you’ve safely connected to the .gov website. Share sensitive information only on official, secure websites.

Crystal Structure of the YjeE Protein from Haemophilus Influenzae: A Putative Atpase Involved in Cell Wall Synthesis

Published

Author(s)

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 since 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. However, the presence of the Walker A motif G-X-X-X-X-G-K-T 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- resolution. The protein has a nucleotide-binding fold with the P-loop typical for many ATPases and GTPases, although the topology of the b-sheet is unique. Crystallization experiments and nucleotide modeling indicate the preference of YjeE to ATP rather than to GTP. The observation of a hydrolyzed nucleotide (ADP) in the active site implies ATPase activity of YjeE. Structural comparison of YjeE with the P-loop proteins from the 14 known families shows that it represents a new class of P-loop ATPases. The phylogenetic pattern of YjeE strongly suggests its involvement in cell wall biosynthesis. The protein is likely to be an ATP-dependent regulator of peptidoglycan metabolism given the distribution of conserved residues and structural features typical for 'molecular switches'. As such, it may be a promising target for new antibiotics.
Citation
Proteins-Structure Function And Genetics
Volume
48
Issue
2

Keywords

ATPase, cell wall synthesis, nucleotide binding fold structural genom

Citation

Teplyakov, A. , Obmolova, G. , Tordova, M. , Thanki, N. , Bonander, N. , Eisenstein, E. , Howard, A. and Gilliland, G. (2002), Crystal Structure of the YjeE Protein from Haemophilus Influenzae: A Putative Atpase Involved in Cell Wall Synthesis, Proteins-Structure Function And Genetics (Accessed April 17, 2024)
Created August 1, 2002, Updated February 19, 2017