2hcb
From Proteopedia
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- | [[Image:2hcb.gif|left|200px]] | + | [[Image:2hcb.gif|left|200px]] |
- | + | ||
- | '''Structure of AMPPCP-bound DnaA from Aquifex aeolicus''' | + | {{Structure |
+ | |PDB= 2hcb |SIZE=350|CAPTION= <scene name='initialview01'>2hcb</scene>, resolution 3.51Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ABG:ADENOSINE 5'-[BETA,GAMMA-METHYLENE]TRIPHOSPHATE'>ABG</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= dnaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 Aquifex aeolicus]) | ||
+ | }} | ||
+ | |||
+ | '''Structure of AMPPCP-bound DnaA from Aquifex aeolicus''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2HCB is a [ | + | 2HCB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HCB OCA]. |
==Reference== | ==Reference== | ||
- | Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling., Erzberger JP, Mott ML, Berger JM, Nat Struct Mol Biol. 2006 Aug;13(8):676-83. Epub 2006 Jul 9. PMID:[http:// | + | Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling., Erzberger JP, Mott ML, Berger JM, Nat Struct Mol Biol. 2006 Aug;13(8):676-83. Epub 2006 Jul 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16829961 16829961] |
[[Category: Aquifex aeolicus]] | [[Category: Aquifex aeolicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: helix-turn-helix]] | [[Category: helix-turn-helix]] | ||
- | ''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 17:15:16 2008'' |
Revision as of 15:15, 20 March 2008
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, resolution 3.51Å | |||||||
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Ligands: | and | ||||||
Gene: | dnaA (Aquifex aeolicus) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Structure of AMPPCP-bound DnaA from Aquifex aeolicus
Overview
In bacteria, the initiation of replication is controlled by DnaA, a member of the ATPases associated with various cellular activities (AAA+) protein superfamily. ATP binding allows DnaA to transition from a monomeric state into a large oligomeric complex that remodels replication origins, triggers duplex melting and facilitates replisome assembly. The crystal structure of AMP-PCP-bound DnaA reveals a right-handed superhelix defined by specific protein-ATP interactions. The observed quaternary structure of DnaA, along with topology footprint assays, indicates that a right-handed DNA wrap is formed around the initiation nucleoprotein complex. This model clarifies how DnaA engages and unwinds bacterial origins and suggests that additional, regulatory AAA+ proteins engage DnaA at filament ends. Eukaryotic and archaeal initiators also have the structural elements that promote open-helix formation, indicating that a spiral, open-ring AAA+ assembly forms the core element of initiators in all domains of life.
About this Structure
2HCB is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.
Reference
Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling., Erzberger JP, Mott ML, Berger JM, Nat Struct Mol Biol. 2006 Aug;13(8):676-83. Epub 2006 Jul 9. PMID:16829961
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