2gxa

From Proteopedia

(Difference between revisions)

Revision as of 11:03, 5 January 2022

Crystal structure of papillomavirus E1 hexameric helicase with ssDNA and MgADP

Structural highlights

2gxa is a 14 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VE1_BPV1] ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Mechanism of DNA translocation in a replicative hexameric helicase.,Enemark EJ, Joshua-Tor L Nature. 2006 Jul 20;442(7100):270-5. PMID:16855583^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Enemark EJ, Joshua-Tor L. Mechanism of DNA translocation in a replicative hexameric helicase. Nature. 2006 Jul 20;442(7100):270-5. PMID:16855583 doi:10.1038/nature04943

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2gxa"

@@ Line 3: / Line 3: @@
 <StructureSection load='2gxa' size='340' side='right'caption='[[2gxa]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2gxa]] is a 14 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GXA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GXA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2gxa]] is a 14 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GXA FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gxa OCA], [http://pdbe.org/2gxa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gxa RCSB], [http://www.ebi.ac.uk/pdbsum/2gxa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2gxa ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gxa OCA], [https://pdbe.org/2gxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gxa RCSB], [https://www.ebi.ac.uk/pdbsum/2gxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gxa ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/VE1_BPV1 VE1_BPV1]] ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins.
+[[https://www.uniprot.org/uniprot/VE1_BPV1 VE1_BPV1]] ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 31: @@
 ==See Also==
 *[[Helicase 3D structures|Helicase 3D structures]]
+*[[Replication protein E1|Replication protein E1]]
 == References ==
 <references/>

2gxa

From Proteopedia

Revision as of 11:03, 5 January 2022

Crystal structure of papillomavirus E1 hexameric helicase with ssDNA and MgADP

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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