1clq
From Proteopedia
(New page: 200px<br /> <applet load="1clq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1clq, resolution 2.70Å" /> '''CRYSTAL STRUCTURE O...) |
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| - | [[Image:1clq.gif|left|200px]]<br /> | + | [[Image:1clq.gif|left|200px]]<br /><applet load="1clq" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1clq" size=" | + | |
caption="1clq, resolution 2.70Å" /> | caption="1clq, resolution 2.70Å" /> | ||
'''CRYSTAL STRUCTURE OF A REPLICATION FORK DNA POLYMERASE EDITING COMPLEX AT 2.7 A RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF A REPLICATION FORK DNA POLYMERASE EDITING COMPLEX AT 2.7 A RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have solved the crystal structures of the bacteriophage RB69 sliding | + | 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== | ||
| - | 1CLQ 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] with CA and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1CLQ with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb3_1.html DNA Polymerase]]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http:// | + | 1CLQ 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] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1CLQ with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb3_1.html DNA Polymerase]]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CLQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Shamoo, Y.]] | [[Category: Shamoo, Y.]] | ||
| - | [[Category: Steitz, T | + | [[Category: Steitz, T A.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: GDP]] | [[Category: GDP]] | ||
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[[Category: replication]] | [[Category: replication]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:19 2008'' |
Revision as of 10:07, 21 February 2008
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CRYSTAL STRUCTURE OF A REPLICATION FORK DNA POLYMERASE EDITING COMPLEX AT 2.7 A RESOLUTION
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.
About this Structure
1CLQ is a Single protein structure of sequence from Enterobacteria phage rb18 with and as ligands. The following page contains interesting information on the relation of 1CLQ with [DNA Polymerase]. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
Reference
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 12:07:19 2008
