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==DnaA N-terminal domain==
The line below this paragraph, containing "STRUCTURE_2e0g", creates the "Structure Box" on the page.
<StructureSection load='2e0g' size='340' side='right'caption='[[2e0g]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2e0g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E0G FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2e0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e0g OCA], [https://pdbe.org/2e0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e0g RCSB], [https://www.ebi.ac.uk/pdbsum/2e0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e0g ProSAT]</span></td></tr>
{{STRUCTURE_2e0g|  PDB=2e0g  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/DNAA_ECOLI DNAA_ECOLI] Plays a key role in the initiation and regulation of chromosomal replication. Binds in an ATP-dependent fashion to the origin of replication (oriC) to initiate formation of the DNA replication initiation complex exactly once per cell cycle. Binds the DnaA box (consensus sequence 5'-TTATC[CA]A[CA]A-3'); subsequent binding of DNA polymerase III subunits leads to replisome formation. The DnaA-ATP form converts to DnaA-ADP; once converted to ADP the protein cannot initiate replication, ensuring only 1 round of replication per cell cycle. DnaA can inhibit its own gene expression as well as that of other genes such as dam, rpoH, ftsA and mioC.<ref>PMID:9242693</ref> <ref>PMID:16077105</ref> <ref>PMID:17699754</ref>  Also required for replication of plasmid DNA; binds 4 dnaA boxes in the minimal plasmid RK2 replication origin (oriV).<ref>PMID:9242693</ref> <ref>PMID:16077105</ref> <ref>PMID:17699754</ref>
== 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/e0/2e0g_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=2e0g ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
DnaA forms a homomultimeric complex with the origin of chromosomal replication (oriC) to unwind duplex DNA. The interaction of the DnaA N terminus with the DnaB helicase is crucial for the loading of DnaB onto the unwound region. Here, we determined the DnaA N terminus structure using NMR. This region (residues 1-108) consists of a rigid region (domain I) and a flexible region (domain II). Domain I has an alpha-alpha-beta-beta-alpha-beta motif, similar to that of the K homology (KH) domain, and has weak affinity for oriC single-stranded DNA, consistent with KH domain function. A hydrophobic surface carrying Trp-6 most likely forms the interface for domain I dimerization. Glu-21 is located on the opposite surface of domain I from the Trp-6 site and is crucial for DnaB helicase loading. These findings suggest a model for DnaA homomultimer formation and DnaB helicase loading on oriC.


'''DnaA N-terminal domain'''
Structure and function of DnaA N-terminal domains: specific sites and mechanisms in inter-DnaA interaction and in DnaB helicase loading on oriC.,Abe Y, Jo T, Matsuda Y, Matsunaga C, Katayama T, Ueda T J Biol Chem. 2007 Jun 15;282(24):17816-27. Epub 2007 Apr 9. PMID:17420252<ref>PMID:17420252</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2e0g" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
2E0G 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=2E0G OCA].
*[[DnaA|DnaA]]
[[Category: Escherichia coli]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Abe, Y.]]
__TOC__
[[Category: Katayama, T.]]
</StructureSection>
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Escherichia coli K-12]]
[[Category: Ueda, T.]]
[[Category: Large Structures]]
[[Category: Domain structure]]
[[Category: Abe Y]]
[[Category: National project on protein structural and functional analyse]]
[[Category: Katayama T]]
[[Category: Nppsfa]]
[[Category: Ueda T]]
[[Category: Riken structural genomics/proteomics initiative]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 01:42:10 2008''

Latest revision as of 08:34, 15 May 2024

DnaA N-terminal domainDnaA N-terminal domain

Structural highlights

2e0g is a 1 chain structure with sequence from Escherichia coli K-12. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DNAA_ECOLI Plays a key role in the initiation and regulation of chromosomal replication. Binds in an ATP-dependent fashion to the origin of replication (oriC) to initiate formation of the DNA replication initiation complex exactly once per cell cycle. Binds the DnaA box (consensus sequence 5'-TTATC[CA]A[CA]A-3'); subsequent binding of DNA polymerase III subunits leads to replisome formation. The DnaA-ATP form converts to DnaA-ADP; once converted to ADP the protein cannot initiate replication, ensuring only 1 round of replication per cell cycle. DnaA can inhibit its own gene expression as well as that of other genes such as dam, rpoH, ftsA and mioC.[1] [2] [3] Also required for replication of plasmid DNA; binds 4 dnaA boxes in the minimal plasmid RK2 replication origin (oriV).[4] [5] [6]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

DnaA forms a homomultimeric complex with the origin of chromosomal replication (oriC) to unwind duplex DNA. The interaction of the DnaA N terminus with the DnaB helicase is crucial for the loading of DnaB onto the unwound region. Here, we determined the DnaA N terminus structure using NMR. This region (residues 1-108) consists of a rigid region (domain I) and a flexible region (domain II). Domain I has an alpha-alpha-beta-beta-alpha-beta motif, similar to that of the K homology (KH) domain, and has weak affinity for oriC single-stranded DNA, consistent with KH domain function. A hydrophobic surface carrying Trp-6 most likely forms the interface for domain I dimerization. Glu-21 is located on the opposite surface of domain I from the Trp-6 site and is crucial for DnaB helicase loading. These findings suggest a model for DnaA homomultimer formation and DnaB helicase loading on oriC.

Structure and function of DnaA N-terminal domains: specific sites and mechanisms in inter-DnaA interaction and in DnaB helicase loading on oriC.,Abe Y, Jo T, Matsuda Y, Matsunaga C, Katayama T, Ueda T J Biol Chem. 2007 Jun 15;282(24):17816-27. Epub 2007 Apr 9. PMID:17420252[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Konieczny I, Doran KS, Helinski DR, Blasina A. Role of TrfA and DnaA proteins in origin opening during initiation of DNA replication of the broad host range plasmid RK2. J Biol Chem. 1997 Aug 8;272(32):20173-8. PMID:9242693
  2. ↑ Riber L, Lobner-Olesen A. Coordinated replication and sequestration of oriC and dnaA are required for maintaining controlled once-per-cell-cycle initiation in Escherichia coli. J Bacteriol. 2005 Aug;187(16):5605-13. PMID:16077105 doi:http://dx.doi.org/10.1128/JB.187.16.5605-5613.2005
  3. ↑ Keyamura K, Fujikawa N, Ishida T, Ozaki S, Su'etsugu M, Fujimitsu K, Kagawa W, Yokoyama S, Kurumizaka H, Katayama T. The interaction of DiaA and DnaA regulates the replication cycle in E. coli by directly promoting ATP DnaA-specific initiation complexes. Genes Dev. 2007 Aug 15;21(16):2083-99. PMID:17699754 doi:21/16/2083
  4. ↑ Konieczny I, Doran KS, Helinski DR, Blasina A. Role of TrfA and DnaA proteins in origin opening during initiation of DNA replication of the broad host range plasmid RK2. J Biol Chem. 1997 Aug 8;272(32):20173-8. PMID:9242693
  5. ↑ Riber L, Lobner-Olesen A. Coordinated replication and sequestration of oriC and dnaA are required for maintaining controlled once-per-cell-cycle initiation in Escherichia coli. J Bacteriol. 2005 Aug;187(16):5605-13. PMID:16077105 doi:http://dx.doi.org/10.1128/JB.187.16.5605-5613.2005
  6. ↑ Keyamura K, Fujikawa N, Ishida T, Ozaki S, Su'etsugu M, Fujimitsu K, Kagawa W, Yokoyama S, Kurumizaka H, Katayama T. The interaction of DiaA and DnaA regulates the replication cycle in E. coli by directly promoting ATP DnaA-specific initiation complexes. Genes Dev. 2007 Aug 15;21(16):2083-99. PMID:17699754 doi:21/16/2083
  7. ↑ Abe Y, Jo T, Matsuda Y, Matsunaga C, Katayama T, Ueda T. Structure and function of DnaA N-terminal domains: specific sites and mechanisms in inter-DnaA interaction and in DnaB helicase loading on oriC. J Biol Chem. 2007 Jun 15;282(24):17816-27. PMID:17420252 doi:10.1074/jbc.M701841200
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