2gxa: Difference between revisions

Revision as of 18:36, 21 February 2008

Crystal structure of papillomavirus E1 hexameric helicase with ssDNA and MgADP

OverviewOverview

The E1 protein of papillomavirus is a hexameric ring helicase belonging to the AAA + family. The mechanism that couples the ATP cycle to DNA translocation has been unclear. Here we present the crystal structure of the E1 hexamer with single-stranded DNA discretely bound within the hexamer channel and nucleotides at the subunit interfaces. This structure demonstrates that only one strand of DNA passes through the hexamer channel and that the DNA-binding hairpins of each subunit form a spiral 'staircase' that sequentially tracks the oligonucleotide backbone. Consecutively grouped ATP, ADP and apo configurations correlate with the height of the hairpin, suggesting a straightforward DNA translocation mechanism. Each subunit sequentially progresses through ATP, ADP and apo states while the associated DNA-binding hairpin travels from the top staircase position to the bottom, escorting one nucleotide of single-stranded DNA through the channel. These events permute sequentially around the ring from one subunit to the next.

About this StructureAbout this Structure

2GXA is a Single protein structure of sequence from Bovine papillomavirus type 1 with , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Mechanism of DNA translocation in a replicative hexameric helicase., Enemark EJ, Joshua-Tor L, Nature. 2006 Jul 20;442(7100):270-5. PMID:16855583

Page seeded by OCA on Thu Feb 21 17:36:16 2008

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OCA

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-[[Image:2gxa.gif|left|200px]]<br /><applet load="2gxa" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2gxa.gif|left|200px]]<br /><applet load="2gxa" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2gxa, resolution 3.15&Aring;" />
 '''Crystal structure of papillomavirus E1 hexameric helicase with ssDNA and MgADP'''<br />
 ==Overview==
-The E1 protein of papillomavirus is a hexameric ring helicase belonging to, the AAA + family. The mechanism that couples the ATP cycle to DNA, translocation has been unclear. Here we present the crystal structure of, the E1 hexamer with single-stranded DNA discretely bound within the, hexamer channel and nucleotides at the subunit interfaces. This structure, demonstrates that only one strand of DNA passes through the hexamer, channel and that the DNA-binding hairpins of each subunit form a spiral, 'staircase' that sequentially tracks the oligonucleotide backbone., Consecutively grouped ATP, ADP and apo configurations correlate with the, height of the hairpin, suggesting a straightforward DNA translocation, mechanism. Each subunit sequentially progresses through ATP, ADP and apo, states while the associated DNA-binding hairpin travels from the top, staircase position to the bottom, escorting one nucleotide of, single-stranded DNA through the channel. These events permute sequentially, around the ring from one subunit to the next.
+The E1 protein of papillomavirus is a hexameric ring helicase belonging to the AAA + family. The mechanism that couples the ATP cycle to DNA translocation has been unclear. Here we present the crystal structure of the E1 hexamer with single-stranded DNA discretely bound within the hexamer channel and nucleotides at the subunit interfaces. This structure demonstrates that only one strand of DNA passes through the hexamer channel and that the DNA-binding hairpins of each subunit form a spiral 'staircase' that sequentially tracks the oligonucleotide backbone. Consecutively grouped ATP, ADP and apo configurations correlate with the height of the hairpin, suggesting a straightforward DNA translocation mechanism. Each subunit sequentially progresses through ATP, ADP and apo states while the associated DNA-binding hairpin travels from the top staircase position to the bottom, escorting one nucleotide of single-stranded DNA through the channel. These events permute sequentially around the ring from one subunit to the next.
 ==About this Structure==
-GXA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bovine_papillomavirus_type_1 Bovine papillomavirus type 1] with MG, CL and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GXA OCA].
+GXA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bovine_papillomavirus_type_1 Bovine papillomavirus type 1] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GXA OCA].
 ==Reference==
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 [[Category: Bovine papillomavirus type 1]]
 [[Category: Single protein]]
-[[Category: Enemark, E.J.]]
+[[Category: Enemark, E J.]]
 [[Category: Joshua-Tor, L.]]
 [[Category: ADP]]
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 [[Category: virus]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:26:28 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:36:16 2008''