2haj

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[[Image:2haj.gif|left|200px]]
[[Image:2haj.gif|left|200px]]
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{{Structure
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|PDB= 2haj |SIZE=350|CAPTION= <scene name='initialview01'>2haj</scene>
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The line below this paragraph, containing "STRUCTURE_2haj", creates the "Structure Box" on the page.
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|GENE= dnaG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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{{STRUCTURE_2haj| PDB=2haj | SCENE= }}
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|RELATEDENTRY=[[1t3w|1T3W]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2haj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2haj OCA], [http://www.ebi.ac.uk/pdbsum/2haj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2haj RCSB]</span>
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'''Solution structure of the helicase-binding domain of Escherichia coli primase'''
'''Solution structure of the helicase-binding domain of Escherichia coli primase'''
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[[Category: Otting, G.]]
[[Category: Otting, G.]]
[[Category: Su, X C.]]
[[Category: Su, X C.]]
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[[Category: dna polymerase]]
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[[Category: Dna polymerase]]
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[[Category: helicase]]
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[[Category: Helicase]]
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[[Category: helix]]
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[[Category: Helix]]
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[[Category: primase]]
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[[Category: Primase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:03:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:27:45 2008''
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Revision as of 03:03, 4 May 2008

Image:2haj.gif

Template:STRUCTURE 2haj

Solution structure of the helicase-binding domain of Escherichia coli primase


Overview

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

2HAJ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 06:03:39 2008

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