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[[Image:2hcb.gif|left|200px]]
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{{STRUCTURE_2hcb|  PDB=2hcb  |  SCENE=  }}
'''Structure of AMPPCP-bound DnaA from Aquifex aeolicus'''


==Structure of AMPPCP-bound DnaA from Aquifex aeolicus==
<StructureSection load='2hcb' size='340' side='right'caption='[[2hcb]], [[Resolution|resolution]] 3.51&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2hcb]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HCB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.51&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hcb OCA], [https://pdbe.org/2hcb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hcb RCSB], [https://www.ebi.ac.uk/pdbsum/2hcb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hcb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DNAA_AQUAE DNAA_AQUAE] Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hc/2hcb_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hcb ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:16829961</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 2hcb" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[DnaA|DnaA]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Berger, J M.]]
[[Category: Berger JM]]
[[Category: Erzberger, J P.]]
[[Category: Erzberger JP]]
[[Category: Mott, M L.]]
[[Category: Mott ML]]
[[Category: Aaa+ atpase]]
[[Category: Helix-turn-helix]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:07:00 2008''

Latest revision as of 09:55, 30 August 2023

Structure of AMPPCP-bound DnaA from Aquifex aeolicus

2hcb, resolution 3.51Å

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