2uvp: Difference between revisions

Revision as of 19:33, 5 November 2007

CRYSTAL STRUCTURE OF HOBA (HP1230)FROM HELICOBACTER PYLORI

OverviewOverview

In prokaryotes, DNA replication is initiated by the binding of DnaA to the, oriC region of the chromosome to load the primosome machinery and start a, new replication round. Several proteins control these events in, Escherichia coli to ensure that replication is precisely timed during the, cell cycle. Here, we report the crystal structure of HobA (HP1230) at 1.7, A, a recently discovered protein that specifically interacts with DnaA, protein from Helicobacter pylori (HpDnaA). We found that the closest, structural homologue of HobA is a sugar isomerase (SIS) domain containing, protein, the phosphoheptose isomerase from Pseudomonas aeruginosa., Remarkably, SIS proteins share strong sequence homology with DiaA from E., coli; yet, HobA and DiaA share no sequence homology. Thus, by solving the, structure of HobA, we unexpectedly discovered that HobA is a H. pylori, structural homologue of DiaA. By comparing the structure of HobA to a, homology model of DiaA, we identified conserved, surface-accessible, residues that could be involved in protein-protein interaction. Finally, we show that HobA specifically interacts with the N-terminal part of, HpDnaA. The structural homology between DiaA and HobA strongly supports, their involvement in the replication process and these proteins could, define a new structural family of replication regulators in bacteria.

About this StructureAbout this Structure

2UVP is a Single protein structure of sequence from Helicobacter pylori with ACT, CA and GOL as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.

ReferenceReference

Structural similarity between the DnaA-binding proteins HobA (HP1230) from Helicobacter pylori and DiaA from Escherichia coli., Natrajan G, Hall DR, Thompson AC, Gutsche I, Terradot L, Mol Microbiol. 2007 Aug;65(4):995-1005. PMID:17683397

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