2od8

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[[Image:2od8.jpg|left|200px]]<br /><applet load="2od8" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2od8.jpg|left|200px]]
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caption="2od8, resolution 2.80&Aring;" />
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'''Structure of a peptide derived from Cdc9 bound to PCNA'''<br />
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{{Structure
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|PDB= 2od8 |SIZE=350|CAPTION= <scene name='initialview01'>2od8</scene>, resolution 2.80&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [http://en.wikipedia.org/wiki/DNA_ligase_(ATP) DNA ligase (ATP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.5.1.1 6.5.1.1]
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|GENE= POL30 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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}}
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'''Structure of a peptide derived from Cdc9 bound to PCNA'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2OD8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/DNA_ligase_(ATP) DNA ligase (ATP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.5.1.1 6.5.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OD8 OCA].
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2OD8 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OD8 OCA].
==Reference==
==Reference==
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The C-terminal domain of yeast PCNA is required for physical and functional interactions with Cdc9 DNA ligase., Vijayakumar S, Chapados BR, Schmidt KH, Kolodner RD, Tainer JA, Tomkinson AE, Nucleic Acids Res. 2007;35(5):1624-37. Epub 2007 Feb 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17308348 17308348]
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The C-terminal domain of yeast PCNA is required for physical and functional interactions with Cdc9 DNA ligase., Vijayakumar S, Chapados BR, Schmidt KH, Kolodner RD, Tainer JA, Tomkinson AE, Nucleic Acids Res. 2007;35(5):1624-37. Epub 2007 Feb 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17308348 17308348]
[[Category: DNA ligase (ATP)]]
[[Category: DNA ligase (ATP)]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: pcna-peptide complex]]
[[Category: pcna-peptide complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:17:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:58:08 2008''

Revision as of 15:58, 20 March 2008


PDB ID 2od8

Drag the structure with the mouse to rotate
, resolution 2.80Å
Gene: POL30 (Saccharomyces cerevisiae)
Activity: DNA ligase (ATP), with EC number 6.5.1.1
Coordinates: save as pdb, mmCIF, xml



Structure of a peptide derived from Cdc9 bound to PCNA


Overview

There is compelling evidence that proliferating cell nuclear antigen (PCNA), a DNA sliding clamp, co-ordinates the processing and joining of Okazaki fragments during eukaryotic DNA replication. However, a detailed mechanistic understanding of functional PCNA:ligase I interactions has been incomplete. Here we present the co-crystal structure of yeast PCNA with a peptide encompassing the conserved PCNA interaction motif of Cdc9, yeast DNA ligase I. The Cdc9 peptide contacts both the inter-domain connector loop (IDCL) and residues near the C-terminus of PCNA. Complementary mutational and biochemical results demonstrate that these two interaction interfaces are required for complex formation both in the absence of DNA and when PCNA is topologically linked to DNA. Similar to the functionally homologous human proteins, yeast RFC interacts with and inhibits Cdc9 DNA ligase whereas the addition of PCNA alleviates inhibition by RFC. Here we show that the ability of PCNA to overcome RFC-mediated inhibition of Cdc9 is dependent upon both the IDCL and the C-terminal interaction interfaces of PCNA. Together these results demonstrate the functional significance of the beta-zipper structure formed between the C-terminal domain of PCNA and Cdc9 and reveal differences in the interactions of FEN-1 and Cdc9 with the two PCNA interfaces that may contribute to the co-ordinated, sequential action of these enzymes.

About this Structure

2OD8 is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The C-terminal domain of yeast PCNA is required for physical and functional interactions with Cdc9 DNA ligase., Vijayakumar S, Chapados BR, Schmidt KH, Kolodner RD, Tainer JA, Tomkinson AE, Nucleic Acids Res. 2007;35(5):1624-37. Epub 2007 Feb 18. PMID:17308348

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