2yva
From Proteopedia
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| - | [[Image:2yva.jpg|left|200px]] | + | [[Image:2yva.jpg|left|200px]] |
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| - | '''Crystal structure of Escherichia coli DiaA''' | + | {{Structure |
| + | |PDB= 2yva |SIZE=350|CAPTION= <scene name='initialview01'>2yva</scene>, resolution 1.85Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= diaA(YraO) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of Escherichia coli DiaA''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2YVA is a [ | + | 2YVA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YVA OCA]. |
==Reference== | ==Reference== | ||
| - | The interaction of DiaA and DnaA regulates the replication cycle in E. coli by directly promoting ATP DnaA-specific initiation complexes., Keyamura K, Fujikawa N, Ishida T, Ozaki S, Su'etsugu M, Fujimitsu K, Kagawa W, Yokoyama S, Kurumizaka H, Katayama T, Genes Dev. 2007 Aug 15;21(16):2083-99. PMID:[http:// | + | The interaction of DiaA and DnaA regulates the replication cycle in E. coli by directly promoting ATP DnaA-specific initiation complexes., Keyamura K, Fujikawa N, Ishida T, Ozaki S, Su'etsugu M, Fujimitsu K, Kagawa W, Yokoyama S, Kurumizaka H, Katayama T, Genes Dev. 2007 Aug 15;21(16):2083-99. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17699754 17699754] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: dnaa binding protein]] | [[Category: dnaa binding protein]] | ||
[[Category: intermolecular disulfide bonding]] | [[Category: intermolecular disulfide bonding]] | ||
| - | [[Category: national project on protein structural and functional | + | [[Category: national project on protein structural and functional analyse]] |
[[Category: nppsfa]] | [[Category: nppsfa]] | ||
[[Category: putative phosphosugar binding protein]] | [[Category: putative phosphosugar binding protein]] | ||
[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:49:30 2008'' |
Revision as of 16:49, 20 March 2008
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| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | diaA(YraO) (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Escherichia coli DiaA
Overview
Escherichia coli DiaA is a DnaA-binding protein that is required for the timely initiation of chromosomal replication during the cell cycle. In this study, we determined the crystal structure of DiaA at 1.8 A resolution. DiaA forms a homotetramer consisting of a symmetrical pair of homodimers. Mutational analysis revealed that the DnaA-binding activity and formation of homotetramers are required for the stimulation of initiation by DiaA. DiaA tetramers can bind multiple DnaA molecules simultaneously. DiaA stimulated the assembly of multiple DnaA molecules on oriC, conformational changes in ATP-DnaA-specific initiation complexes, and unwinding of oriC duplex DNA. The mutant DiaA proteins are defective in these stimulations. DiaA associated also with ADP-DnaA, and stimulated the assembly of inactive ADP-DnaA-oriC complexes. Specific residues in the putative phosphosugar-binding motif of DiaA were required for the stimulation of initiation and formation of ATP-DnaA-specific-oriC complexes. Our data indicate that DiaA regulates initiation by a novel mechanism, in which DiaA tetramers most likely bind to multiple DnaA molecules and stimulate the assembly of specific ATP-DnaA-oriC complexes. These results suggest an essential role for DiaA in the promotion of replication initiation in a cell cycle coordinated manner.
About this Structure
2YVA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The interaction of DiaA and DnaA regulates the replication cycle in E. coli by directly promoting ATP DnaA-specific initiation complexes., Keyamura K, Fujikawa N, Ishida T, Ozaki S, Su'etsugu M, Fujimitsu K, Kagawa W, Yokoyama S, Kurumizaka H, Katayama T, Genes Dev. 2007 Aug 15;21(16):2083-99. PMID:17699754
Page seeded by OCA on Thu Mar 20 18:49:30 2008
Categories: Escherichia coli | Single protein | Fujikawa, N. | Ishida, T. | Kagawa, W. | Katayama, T. | Keyamura, K. | Kurumizaka, H. | Ozaki, S. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Suetsugu, M. | Yokoyama, S. | Dna binding protein | Dnaa binding protein | Intermolecular disulfide bonding | National project on protein structural and functional analyse | Nppsfa | Putative phosphosugar binding protein | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic
