1b77: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1b77" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b77, resolution 2.10Å" /> '''BUILDING A REPLISOME...
 
No edit summary
Line 1: Line 1:
[[Image:1b77.gif|left|200px]]<br /><applet load="1b77" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1b77.gif|left|200px]]<br /><applet load="1b77" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1b77, resolution 2.10&Aring;" />
caption="1b77, resolution 2.10&Aring;" />
'''BUILDING A REPLISOME STRUCTURE FROM INTERACTING PIECES: A SLIDING CLAMP COMPLEXED WITH AN INTERACTION PEPTIDE FROM DNA POLYMERASE'''<br />
'''BUILDING A REPLISOME STRUCTURE FROM INTERACTING PIECES: A SLIDING CLAMP COMPLEXED WITH AN INTERACTION PEPTIDE FROM DNA POLYMERASE'''<br />


==Overview==
==Overview==
We have solved the crystal structures of the bacteriophage RB69 sliding, clamp, its complex with a peptide essential for DNA polymerase, interactions, and the DNA polymerase complexed with primer-template DNA., The editing complex structure shows a partially melted duplex DNA exiting, from the exonuclease domain at an unexpected angle and significant changes, in the protein structure. The clamp complex shows the C-terminal 11, residues of polymerase bound in a hydrophobic pocket, and it allows, docking of the editing and clamp structures together. The peptide binds to, the sliding clamp at a position identical to that of a replication, inhibitor peptide bound to PCNA, suggesting that the replication inhibitor, protein p21CIP1 functions by competing with eukaryotic polymerases for the, same binding pocket on the clamp.
We have solved the crystal structures of the bacteriophage RB69 sliding clamp, its complex with a peptide essential for DNA polymerase interactions, and the DNA polymerase complexed with primer-template DNA. The editing complex structure shows a partially melted duplex DNA exiting from the exonuclease domain at an unexpected angle and significant changes in the protein structure. The clamp complex shows the C-terminal 11 residues of polymerase bound in a hydrophobic pocket, and it allows docking of the editing and clamp structures together. The peptide binds to the sliding clamp at a position identical to that of a replication inhibitor peptide bound to PCNA, suggesting that the replication inhibitor protein p21CIP1 functions by competing with eukaryotic polymerases for the same binding pocket on the clamp.


==About this Structure==
==About this Structure==
1B77 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_rb18 Enterobacteria phage rb18]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B77 OCA].  
1B77 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_rb18 Enterobacteria phage rb18]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B77 OCA].  


==Reference==
==Reference==
Line 14: Line 14:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Shamoo, Y.]]
[[Category: Shamoo, Y.]]
[[Category: Steitz, T.A.]]
[[Category: Steitz, T A.]]
[[Category: gp45]]
[[Category: gp45]]
[[Category: replisome]]
[[Category: replisome]]
[[Category: sliding clamp]]
[[Category: sliding clamp]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:25:16 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:15 2008''

Revision as of 12:52, 21 February 2008

File:1b77.gif


1b77, resolution 2.10Å

Drag the structure with the mouse to rotate

BUILDING A REPLISOME STRUCTURE FROM INTERACTING PIECES: A SLIDING CLAMP COMPLEXED WITH AN INTERACTION PEPTIDE FROM DNA POLYMERASE

OverviewOverview

We have solved the crystal structures of the bacteriophage RB69 sliding clamp, its complex with a peptide essential for DNA polymerase interactions, and the DNA polymerase complexed with primer-template DNA. The editing complex structure shows a partially melted duplex DNA exiting from the exonuclease domain at an unexpected angle and significant changes in the protein structure. The clamp complex shows the C-terminal 11 residues of polymerase bound in a hydrophobic pocket, and it allows docking of the editing and clamp structures together. The peptide binds to the sliding clamp at a position identical to that of a replication inhibitor peptide bound to PCNA, suggesting that the replication inhibitor protein p21CIP1 functions by competing with eukaryotic polymerases for the same binding pocket on the clamp.

About this StructureAbout this Structure

1B77 is a Single protein structure of sequence from Enterobacteria phage rb18. Full crystallographic information is available from OCA.

ReferenceReference

Building a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex., Shamoo Y, Steitz TA, Cell. 1999 Oct 15;99(2):155-66. PMID:10535734

Page seeded by OCA on Thu Feb 21 11:52:15 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA