2uvp
From Proteopedia
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==Overview== | ==Overview== | ||
| - | In prokaryotes, DNA replication is initiated by the binding of DnaA to the | + | 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 Structure== | ==About this Structure== | ||
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[[Category: Helicobacter pylori]] | [[Category: Helicobacter pylori]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hall, D | + | [[Category: Hall, D R.]] |
[[Category: Natrajan, G.]] | [[Category: Natrajan, G.]] | ||
[[Category: Terradot, L.]] | [[Category: Terradot, L.]] | ||
| - | [[Category: Thompson, A | + | [[Category: Thompson, A C.]] |
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: unknown function]] | [[Category: unknown function]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:50:45 2008'' |
Revision as of 16:50, 21 February 2008
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CRYSTAL STRUCTURE OF HOBA (HP1230)FROM HELICOBACTER PYLORI
Overview
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 Structure
2UVP is a Single protein structure of sequence from Helicobacter pylori with , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 18:50:45 2008
Categories: Helicobacter pylori | Single protein | Hall, D R. | Natrajan, G. | Terradot, L. | Thompson, A C. | ACT | CA | GOL | Dna replication | Dnaa | Hypothetical protein | Sis fold | Unknown function
