2hcb
From Proteopedia
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|PDB= 2hcb |SIZE=350|CAPTION= <scene name='initialview01'>2hcb</scene>, resolution 3.51Å | |PDB= 2hcb |SIZE=350|CAPTION= <scene name='initialview01'>2hcb</scene>, resolution 3.51Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=ABG:ADENOSINE+5'-[BETA,GAMMA-METHYLENE]TRIPHOSPHATE'>ABG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= dnaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 Aquifex aeolicus]) | |GENE= dnaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 Aquifex aeolicus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hcb OCA], [http://www.ebi.ac.uk/pdbsum/2hcb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hcb RCSB]</span> | ||
}} | }} | ||
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[[Category: Erzberger, J P.]] | [[Category: Erzberger, J P.]] | ||
[[Category: Mott, M L.]] | [[Category: Mott, M L.]] | ||
| - | [[Category: ABG]] | ||
| - | [[Category: MG]] | ||
[[Category: aaa+ atpase]] | [[Category: aaa+ atpase]] | ||
[[Category: helix-turn-helix]] | [[Category: helix-turn-helix]] | ||
| - | ''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 03:28:30 2008'' |
Revision as of 00:28, 31 March 2008
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| , resolution 3.51Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | dnaA (Aquifex aeolicus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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