1t3w
From Proteopedia
(New page: 200px<br /><applet load="1t3w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t3w, resolution 2.80Å" /> '''Crystal Structure of...) |
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| - | [[Image:1t3w.jpg|left|200px]]<br /><applet load="1t3w" size=" | + | [[Image:1t3w.jpg|left|200px]]<br /><applet load="1t3w" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1t3w, resolution 2.80Å" /> | caption="1t3w, resolution 2.80Å" /> | ||
'''Crystal Structure of the E.coli DnaG C-terminal domain (residues 434 to 581)'''<br /> | '''Crystal Structure of the E.coli DnaG C-terminal domain (residues 434 to 581)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | During bacterial DNA replication, the DnaG primase interacts with the | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1T3W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ACY as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1T3W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T3W OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dixon, N | + | [[Category: Dixon, N E.]] |
[[Category: Liepinsh, E.]] | [[Category: Liepinsh, E.]] | ||
| - | [[Category: Loscha, K | + | [[Category: Loscha, K V.]] |
| - | [[Category: Oakley, A | + | [[Category: Oakley, A J.]] |
[[Category: Otting, G.]] | [[Category: Otting, G.]] | ||
| - | [[Category: Schaeffer, P | + | [[Category: Schaeffer, P M.]] |
| - | [[Category: Wilce, M | + | [[Category: Wilce, M C.J.]] |
[[Category: ACY]] | [[Category: ACY]] | ||
[[Category: dna replication]] | [[Category: dna replication]] | ||
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[[Category: e. coli]] | [[Category: e. coli]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:09:34 2008'' |
Revision as of 13:09, 21 February 2008
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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.
About this Structure
1T3W is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
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:15649896
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