1t3w: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1t3w.jpg|left|200px]]
{{Seed}}
[[Image:1t3w.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1t3w|  PDB=1t3w  |  SCENE=  }}  
{{STRUCTURE_1t3w|  PDB=1t3w  |  SCENE=  }}  


'''Crystal Structure of the E.coli DnaG C-terminal domain (residues 434 to 581)'''
===Crystal Structure of the E.coli DnaG C-terminal domain (residues 434 to 581)===




==Overview==
<!--
During bacterial DNA replication, the DnaG primase interacts with the hexameric DnaB helicase to synthesize RNA primers for extension by DNA polymerase. In Escherichia coli, this occurs by transient interaction of primase with the helicase. Here we demonstrate directly by surface plasmon resonance that the C-terminal domain of primase is responsible for interaction with DnaB6. Determination of the 2.8-angstroms crystal structure of the C-terminal domain of primase revealed an asymmetric dimer. The monomers have an N-terminal helix bundle similar to the N-terminal domain of DnaB, followed by a long helix that connects to a C-terminal helix hairpin. The connecting helix is interrupted differently in the two monomers. Solution studies using NMR showed that an equilibrium exists between a monomeric species with an intact, extended but naked, connecting helix and a dimer in which this helix is interrupted in the same way as in one of the crystal conformers. The other conformer is not significantly populated in solution, and its presence in the crystal is due largely to crystal packing forces. It is proposed that the connecting helix contributes necessary structural flexibility in the primase-helicase complex at replication forks.
The line below this paragraph, {{ABSTRACT_PUBMED_15649896}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15649896 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15649896}}


==About this Structure==
==About this Structure==
Line 20: Line 24:
==Reference==
==Reference==
Crystal and solution structures of the helicase-binding domain of Escherichia coli primase., Oakley AJ, Loscha KV, Schaeffer PM, Liepinsh E, Pintacuda G, Wilce MC, Otting G, Dixon NE, J Biol Chem. 2005 Mar 25;280(12):11495-504. Epub 2005 Jan 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15649896 15649896]
Crystal and solution structures of the helicase-binding domain of Escherichia coli primase., Oakley AJ, Loscha KV, Schaeffer PM, Liepinsh E, Pintacuda G, Wilce MC, Otting G, Dixon NE, J Biol Chem. 2005 Mar 25;280(12):11495-504. Epub 2005 Jan 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15649896 15649896]
Expression, purification, crystallization, and NMR studies of the helicase interaction domain of Escherichia coli DnaG primase., Loscha K, Oakley AJ, Bancia B, Schaeffer PM, Prosselkov P, Otting G, Wilce MC, Dixon NE, Protein Expr Purif. 2004 Feb;33(2):304-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14711519 14711519]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 33: Line 39:
[[Category: Dnag]]
[[Category: Dnag]]
[[Category: E. coli]]
[[Category: E. coli]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:29:28 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:50:30 2008''
Retrieved from "https://proteopedia.org/1t3w"