1b77: Difference between revisions

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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...
 
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[[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==
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[[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''