2haj
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:2haj.png|left|200px]] | ||
- | < | + | ==Solution structure of the helicase-binding domain of Escherichia coli primase== |
- | + | <StructureSection load='2haj' size='340' side='right'caption='[[2haj]]' scene=''> | |
- | You may | + | == 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> | |
- | or | + | </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. | ||
- | + | 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> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 2haj" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | |
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: Dixon | + | [[Category: Dixon NE]] |
- | [[Category: Loscha | + | [[Category: Loscha KV]] |
- | [[Category: Otting | + | [[Category: Otting G]] |
- | [[Category: Su | + | [[Category: Su XC]] |
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Current revision
Solution structure of the helicase-binding domain of Escherichia coli primase
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