2hii

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(New page: 200px<br /><applet load="2hii" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hii, resolution 2.79&Aring;" /> '''heterotrimeric PCNA ...)
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[[Image:2hii.jpg|left|200px]]<br /><applet load="2hii" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2hii.jpg|left|200px]]<br /><applet load="2hii" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2hii, resolution 2.79&Aring;" />
caption="2hii, resolution 2.79&Aring;" />
'''heterotrimeric PCNA sliding clamp'''<br />
'''heterotrimeric PCNA sliding clamp'''<br />
==Overview==
==Overview==
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DNA sliding clamps encircle DNA and provide binding sites for many, DNA-processing enzymes. However, it is largely unknown how sliding clamps, like proliferating cell nuclear antigen (PCNA) coordinate multistep DNA, transactions. We have determined structures of Sulfolobus solfataricus DNA, ligase and heterotrimeric PCNA separately by X-ray diffraction and in, complex by small-angle X-ray scattering (SAXS). Three distinct PCNA, subunits assemble into a protein ring resembling the homotrimeric PCNA of, humans but with three unique protein-binding sites. In the absence of, nicked DNA, the Sulfolobus solfataricus DNA ligase has an open, extended, conformation. When complexed with heterotrimeric PCNA, the DNA ligase, binds to the PCNA3 subunit and ligase retains an open, extended, conformation. A closed, ring-shaped conformation of ligase catalyzes a DNA, end-joining reaction that is strongly stimulated by PCNA. This, open-to-closed switch in the conformation of DNA ligase is accommodated by, a malleable interface with PCNA that serves as an efficient platform for, DNA ligation.
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DNA sliding clamps encircle DNA and provide binding sites for many DNA-processing enzymes. However, it is largely unknown how sliding clamps like proliferating cell nuclear antigen (PCNA) coordinate multistep DNA transactions. We have determined structures of Sulfolobus solfataricus DNA ligase and heterotrimeric PCNA separately by X-ray diffraction and in complex by small-angle X-ray scattering (SAXS). Three distinct PCNA subunits assemble into a protein ring resembling the homotrimeric PCNA of humans but with three unique protein-binding sites. In the absence of nicked DNA, the Sulfolobus solfataricus DNA ligase has an open, extended conformation. When complexed with heterotrimeric PCNA, the DNA ligase binds to the PCNA3 subunit and ligase retains an open, extended conformation. A closed, ring-shaped conformation of ligase catalyzes a DNA end-joining reaction that is strongly stimulated by PCNA. This open-to-closed switch in the conformation of DNA ligase is accommodated by a malleable interface with PCNA that serves as an efficient platform for DNA ligation.
==About this Structure==
==About this Structure==
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2HII is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HII OCA].
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2HII is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HII OCA].
==Reference==
==Reference==
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[[Category: Sulfolobus solfataricus]]
[[Category: Sulfolobus solfataricus]]
[[Category: Ellenberger, T.]]
[[Category: Ellenberger, T.]]
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[[Category: Pascal, J.M.]]
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[[Category: Pascal, J M.]]
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[[Category: Tsodikov, O.V.]]
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[[Category: Tsodikov, O V.]]
[[Category: dna replication]]
[[Category: dna replication]]
[[Category: heterotrimeric]]
[[Category: heterotrimeric]]
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[[Category: sliding clamp]]
[[Category: sliding clamp]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:47:21 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:42:26 2008''

Revision as of 15:42, 21 February 2008


2hii, resolution 2.79Å

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heterotrimeric PCNA sliding clamp

Overview

DNA sliding clamps encircle DNA and provide binding sites for many DNA-processing enzymes. However, it is largely unknown how sliding clamps like proliferating cell nuclear antigen (PCNA) coordinate multistep DNA transactions. We have determined structures of Sulfolobus solfataricus DNA ligase and heterotrimeric PCNA separately by X-ray diffraction and in complex by small-angle X-ray scattering (SAXS). Three distinct PCNA subunits assemble into a protein ring resembling the homotrimeric PCNA of humans but with three unique protein-binding sites. In the absence of nicked DNA, the Sulfolobus solfataricus DNA ligase has an open, extended conformation. When complexed with heterotrimeric PCNA, the DNA ligase binds to the PCNA3 subunit and ligase retains an open, extended conformation. A closed, ring-shaped conformation of ligase catalyzes a DNA end-joining reaction that is strongly stimulated by PCNA. This open-to-closed switch in the conformation of DNA ligase is accommodated by a malleable interface with PCNA that serves as an efficient platform for DNA ligation.

About this Structure

2HII is a Protein complex structure of sequences from Sulfolobus solfataricus. Full crystallographic information is available from OCA.

Reference

A flexible interface between DNA ligase and PCNA supports conformational switching and efficient ligation of DNA., Pascal JM, Tsodikov OV, Hura GL, Song W, Cotner EA, Classen S, Tomkinson AE, Tainer JA, Ellenberger T, Mol Cell. 2006 Oct 20;24(2):279-91. PMID:17052461

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