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

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TitleCrystal structure of the YjeE protein from Haemophilus influenzae: a putative Atpase involved in cell wall synthesis.
Publication TypeJournal Article
Year of Publication2002
AuthorsTeplyakov, A, Obmolova, G, Tordova, M, Thanki, N, Bonander, N, Eisenstein, E, Howard, AJ, Gilliland, GL
JournalProteins
Volume48
Issue2
Pagination220-6
Date Published2002 Aug 1
ISSN1097-0134
KeywordsAdenosine Triphosphatases, Amino Acid Sequence, Bacterial Proteins, Cell Wall, Crystallography, X-Ray, Haemophilus influenzae, Models, Molecular, Molecular Sequence Data, Nucleotides, Phylogeny, Sequence Homology, Amino Acid
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.

DOI10.1002/prot.10114
Alternate JournalProteins
PubMed ID12112691
Grant ListP01-GM57890 / GM / NIGMS NIH HHS / United States