1f08

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(New page: 200px<br /><applet load="1f08" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f08, resolution 1.90&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1f08.gif|left|200px]]<br /><applet load="1f08" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1f08.gif|left|200px]]<br /><applet load="1f08" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1f08, resolution 1.90&Aring;" />
caption="1f08, resolution 1.90&Aring;" />
'''CRYSTAL STRUCTURE OF THE DNA-BINDING DOMAIN OF THE REPLICATION INITIATION PROTEIN E1 FROM PAPILLOMAVIRUS'''<br />
'''CRYSTAL STRUCTURE OF THE DNA-BINDING DOMAIN OF THE REPLICATION INITIATION PROTEIN E1 FROM PAPILLOMAVIRUS'''<br />
==Overview==
==Overview==
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Papillomaviral infection causes both benign and malignant lesions and is a, necessary cause of cervical carcinoma. Replication of this virus requires, the replication initiation proteins E1 and E2, which bind cooperatively at, the origin of replication (ori) as an (E1)2-(E2)2-DNA complex. This is a, precursor to larger E1 complexes that distort and unwind the ori. We, present the crystal structure of the E1 DNA binding domain refined to 1.9, A resolution. Residues critical for DNA binding are located on an extended, loop and an alpha helix. We identify the E1 dimerization surface by, selective mutations at an E1/E1 interface observed in the crystal and, propose a model for the (E1)2-DNA complex. These and other observations, suggest how the E1 DNA binding domain orchestrates assembly of the, hexameric helicase on the ori.
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Papillomaviral infection causes both benign and malignant lesions and is a necessary cause of cervical carcinoma. Replication of this virus requires the replication initiation proteins E1 and E2, which bind cooperatively at the origin of replication (ori) as an (E1)2-(E2)2-DNA complex. This is a precursor to larger E1 complexes that distort and unwind the ori. We present the crystal structure of the E1 DNA binding domain refined to 1.9 A resolution. Residues critical for DNA binding are located on an extended loop and an alpha helix. We identify the E1 dimerization surface by selective mutations at an E1/E1 interface observed in the crystal and propose a model for the (E1)2-DNA complex. These and other observations suggest how the E1 DNA binding domain orchestrates assembly of the hexameric helicase on the ori.
==About this Structure==
==About this Structure==
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1F08 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bovine_papillomavirus Bovine papillomavirus] with BR as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F08 OCA].
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1F08 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bovine_papillomavirus Bovine papillomavirus] with <scene name='pdbligand=BR:'>BR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F08 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chen, G.]]
[[Category: Chen, G.]]
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[[Category: Enemark, E.J.]]
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[[Category: Enemark, E J.]]
[[Category: Joshua-Tor, L.]]
[[Category: Joshua-Tor, L.]]
[[Category: Stenlund, A.]]
[[Category: Stenlund, A.]]
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[[Category: Vaughn, D.E.]]
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[[Category: Vaughn, D E.]]
[[Category: BR]]
[[Category: BR]]
[[Category: dna-binding domain]]
[[Category: dna-binding domain]]
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[[Category: replication]]
[[Category: replication]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:29:28 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:23 2008''

Revision as of 10:33, 21 February 2008


1f08, resolution 1.90Å

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CRYSTAL STRUCTURE OF THE DNA-BINDING DOMAIN OF THE REPLICATION INITIATION PROTEIN E1 FROM PAPILLOMAVIRUS

Overview

Papillomaviral infection causes both benign and malignant lesions and is a necessary cause of cervical carcinoma. Replication of this virus requires the replication initiation proteins E1 and E2, which bind cooperatively at the origin of replication (ori) as an (E1)2-(E2)2-DNA complex. This is a precursor to larger E1 complexes that distort and unwind the ori. We present the crystal structure of the E1 DNA binding domain refined to 1.9 A resolution. Residues critical for DNA binding are located on an extended loop and an alpha helix. We identify the E1 dimerization surface by selective mutations at an E1/E1 interface observed in the crystal and propose a model for the (E1)2-DNA complex. These and other observations suggest how the E1 DNA binding domain orchestrates assembly of the hexameric helicase on the ori.

About this Structure

1F08 is a Single protein structure of sequence from Bovine papillomavirus with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the DNA binding domain of the replication initiation protein E1 from papillomavirus., Enemark EJ, Chen G, Vaughn DE, Stenlund A, Joshua-Tor L, Mol Cell. 2000 Jul;6(1):149-58. PMID:10949036

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