2haj

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(New page: 200px<br /><applet load="2haj" size="450" color="white" frame="true" align="right" spinBox="true" caption="2haj" /> '''Solution structure of the helicase-binding d...)
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[[Image:2haj.gif|left|200px]]<br /><applet load="2haj" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Solution structure of the helicase-binding domain of Escherichia coli primase'''<br />
'''Solution structure of the helicase-binding domain of Escherichia coli primase'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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2HAJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HAJ OCA].
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2HAJ is a [http://en.wikipedia.org/wiki/Single_protein 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].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Dixon, N.E.]]
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[[Category: Dixon, N E.]]
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[[Category: Loscha, K.V.]]
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[[Category: Loscha, K V.]]
[[Category: Otting, G.]]
[[Category: Otting, G.]]
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[[Category: Su, X.C.]]
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[[Category: Su, X C.]]
[[Category: dna polymerase]]
[[Category: dna polymerase]]
[[Category: helicase]]
[[Category: helicase]]
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[[Category: primase]]
[[Category: primase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:38:38 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:39:52 2008''

Revision as of 15:39, 21 February 2008

Image:2haj.gif

2haj

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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

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