2uvp
From Proteopedia
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|PDB= 2uvp |SIZE=350|CAPTION= <scene name='initialview01'>2uvp</scene>, resolution 1.70Å | |PDB= 2uvp |SIZE=350|CAPTION= <scene name='initialview01'>2uvp</scene>, resolution 1.70Å | ||
|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2uvp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uvp OCA], [http://www.ebi.ac.uk/pdbsum/2uvp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2uvp RCSB]</span> | ||
}} | }} | ||
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[[Category: Terradot, L.]] | [[Category: Terradot, L.]] | ||
[[Category: Thompson, A C.]] | [[Category: Thompson, A C.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: GOL]] | ||
[[Category: dna replication]] | [[Category: dna replication]] | ||
[[Category: dnaa]] | [[Category: dnaa]] | ||
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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 Mon Mar 31 05:05:07 2008'' |
Revision as of 02:05, 31 March 2008
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| , resolution 1.70Å | |||||||
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| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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