2haj: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2haj.gif|left|200px]] | [[Image:2haj.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_2haj", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{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''' | ||
| Line 29: | Line 26: | ||
[[Category: Otting, G.]] | [[Category: Otting, G.]] | ||
[[Category: Su, X C.]] | [[Category: Su, X C.]] | ||
[[Category: | [[Category: Dna polymerase]] | ||
[[Category: | [[Category: Helicase]] | ||
[[Category: | [[Category: Helix]] | ||
[[Category: | [[Category: Primase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:03:39 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 03:03, 4 May 2008
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
