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[[Image:2haj.gif|left|200px]]
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{{STRUCTURE_2haj|  PDB=2haj  |  SCENE=  }}
'''Solution structure of the helicase-binding domain of Escherichia coli primase'''


==Solution structure of the helicase-binding domain of Escherichia coli primase==
<StructureSection load='2haj' size='340' side='right'caption='[[2haj]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2haj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HAJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HAJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2haj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2haj OCA], [https://pdbe.org/2haj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2haj RCSB], [https://www.ebi.ac.uk/pdbsum/2haj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2haj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DNAG_ECOLI DNAG_ECOLI] RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.[HAMAP-Rule:MF_00974]<ref>PMID:1511009</ref> <ref>PMID:340457</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/ha/2haj_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=2haj ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
DnaG is the primase that lays down RNA primers on single-stranded DNA during bacterial DNA replication. The solution structure of the DnaB-helicase-binding C-terminal domain of Escherichia coli DnaG was determined by NMR spectroscopy at near-neutral pH. The structure is a rare fold that, besides occurring in DnaG C-terminal domains, has been described only for the N-terminal domain of DnaB. The C-terminal helix hairpin present in the DnaG C-terminal domain, however, is either less stable or absent in DnaB, as evidenced by high mobility of the C-terminal 35 residues in a construct comprising residues 1-171. The present structure identifies the previous crystal structure of the E. coli DnaG C-terminal domain as a domain-swapped dimer. It is also significantly different from the NMR structure reported for the corresponding domain of DnaG from the thermophile Bacillus stearothermophilus. NMR experiments showed that the DnaG C-terminal domain does not bind to residues 1-171 of the E. coli DnaB helicase with significant affinity.


==Overview==
Monomeric solution structure of the helicase-binding domain of Escherichia coli DnaG primase.,Su XC, Schaeffer PM, Loscha KV, Gan PH, Dixon NE, Otting G FEBS J. 2006 Nov;273(21):4997-5009. Epub 2006 Sep 28. PMID:17010164<ref>PMID:17010164</ref>
DnaG is the primase that lays down RNA primers on single-stranded DNA during bacterial DNA replication. The solution structure of the DnaB-helicase-binding C-terminal domain of Escherichia coli DnaG was determined by NMR spectroscopy at near-neutral pH. The structure is a rare fold that, besides occurring in DnaG C-terminal domains, has been described only for the N-terminal domain of DnaB. The C-terminal helix hairpin present in the DnaG C-terminal domain, however, is either less stable or absent in DnaB, as evidenced by high mobility of the C-terminal 35 residues in a construct comprising residues 1-171. The present structure identifies the previous crystal structure of the E. coli DnaG C-terminal domain as a domain-swapped dimer. It is also significantly different from the NMR structure reported for the corresponding domain of DnaG from the thermophile Bacillus stearothermophilus. NMR experiments showed that the DnaG C-terminal domain does not bind to residues 1-171 of the E. coli DnaB helicase with significant affinity.


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


==Reference==
==See Also==
Monomeric solution structure of the helicase-binding domain of Escherichia coli DnaG primase., Su XC, Schaeffer PM, Loscha KV, Gan PH, Dixon NE, Otting G, FEBS J. 2006 Nov;273(21):4997-5009. Epub 2006 Sep 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17010164 17010164]
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Dixon, N E.]]
[[Category: Dixon NE]]
[[Category: Loscha, K V.]]
[[Category: Loscha KV]]
[[Category: Otting, G.]]
[[Category: Otting G]]
[[Category: Su, X C.]]
[[Category: Su XC]]
[[Category: Dna polymerase]]
[[Category: Helicase]]
[[Category: Helix]]
[[Category: Primase]]
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Retrieved from "https://proteopedia.org/2haj"