2va8
From Proteopedia
(New page: 200px<br /><applet load="2va8" size="350" color="white" frame="true" align="right" spinBox="true" caption="2va8, resolution 2.30Å" /> '''DNA REPAIR HELICASE ...) |
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==Overview== | ==Overview== | ||
| - | Hel308 is a superfamily 2 helicase conserved in eukaryotes and archaea. It | + | Hel308 is a superfamily 2 helicase conserved in eukaryotes and archaea. It is thought to function in the early stages of recombination following replication fork arrest and has a specificity for removal of the lagging strand in model replication forks. A homologous helicase constitutes the N-terminal domain of human DNA polymerase Q. The Drosophila homologue mus301 is implicated in double strand break repair and meiotic recombination. We have solved the high resolution crystal structure of Hel308 from the crenarchaeon Sulfolobus solfataricus, revealing a five-domain structure with a central pore lined with essential DNA binding residues. The fifth domain is shown to act as an autoinhibitory domain or molecular brake, clamping the single-stranded DNA extruded through the central pore of the helicase structure to limit the helicase activity of the enzyme. This provides an elegant mechanism to tune the processivity of the enzyme to its functional role. Hel308 can displace streptavidin from a biotinylated DNA molecule, and this activity is only partially inhibited when the DNA is pre-bound with abundant DNA-binding proteins RPA or Alba1, whereas pre-binding with the recombinase RadA has no effect on activity. These data suggest that one function of the enzyme may be in the removal of bound proteins at stalled replication forks and recombination intermediates. |
==About this Structure== | ==About this Structure== | ||
| - | 2VA8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=AC1:So4 Binding Site For Chain A'>AC1</scene>, <scene name='pdbsite=AC2:So4 Binding Site For Chain A'>AC2</scene>, <scene name='pdbsite=AC3:So4 Binding Site For Chain B'>AC3</scene>, <scene name='pdbsite=AC4:So4 Binding Site For Chain B'>AC4</scene>, <scene name='pdbsite=AC5:So4 Binding Site For Chain B'>AC5</scene>, <scene name='pdbsite=AC6:So4 Binding Site For Chain B'>AC6</scene> and <scene name='pdbsite=AC7:So4 Binding Site For Chain B'>AC7</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VA8 OCA]. | + | 2VA8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Chain+B'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Chain+B'>AC4</scene>, <scene name='pdbsite=AC5:So4+Binding+Site+For+Chain+B'>AC5</scene>, <scene name='pdbsite=AC6:So4+Binding+Site+For+Chain+B'>AC6</scene> and <scene name='pdbsite=AC7:So4+Binding+Site+For+Chain+B'>AC7</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VA8 OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the DNA repair helicase | + | Structure of the DNA repair helicase hel308 reveals DNA binding and autoinhibitory domains., Richards JD, Johnson KA, Liu H, McRobbie AM, McMahon S, Oke M, Carter L, Naismith JH, White MF, J Biol Chem. 2008 Feb 22;283(8):5118-26. Epub 2007 Dec 4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18056710 18056710] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sulfolobus solfataricus]] | [[Category: Sulfolobus solfataricus]] | ||
[[Category: Carter, L.]] | [[Category: Carter, L.]] | ||
| - | [[Category: Johnson, K | + | [[Category: Johnson, K A.]] |
[[Category: Liu, H.]] | [[Category: Liu, H.]] | ||
[[Category: Mcmahon, S.]] | [[Category: Mcmahon, S.]] | ||
| - | [[Category: Naismith, J | + | [[Category: Naismith, J H.]] |
[[Category: Oke, M.]] | [[Category: Oke, M.]] | ||
[[Category: Richards, J.]] | [[Category: Richards, J.]] | ||
| - | [[Category: White, M | + | [[Category: White, M F.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: atp-binding]] | [[Category: atp-binding]] | ||
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[[Category: sso2462]] | [[Category: sso2462]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:54:31 2008'' |
Revision as of 16:54, 21 February 2008
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DNA REPAIR HELICASE HEL308
Overview
Hel308 is a superfamily 2 helicase conserved in eukaryotes and archaea. It is thought to function in the early stages of recombination following replication fork arrest and has a specificity for removal of the lagging strand in model replication forks. A homologous helicase constitutes the N-terminal domain of human DNA polymerase Q. The Drosophila homologue mus301 is implicated in double strand break repair and meiotic recombination. We have solved the high resolution crystal structure of Hel308 from the crenarchaeon Sulfolobus solfataricus, revealing a five-domain structure with a central pore lined with essential DNA binding residues. The fifth domain is shown to act as an autoinhibitory domain or molecular brake, clamping the single-stranded DNA extruded through the central pore of the helicase structure to limit the helicase activity of the enzyme. This provides an elegant mechanism to tune the processivity of the enzyme to its functional role. Hel308 can displace streptavidin from a biotinylated DNA molecule, and this activity is only partially inhibited when the DNA is pre-bound with abundant DNA-binding proteins RPA or Alba1, whereas pre-binding with the recombinase RadA has no effect on activity. These data suggest that one function of the enzyme may be in the removal of bound proteins at stalled replication forks and recombination intermediates.
About this Structure
2VA8 is a Single protein structure of sequence from Sulfolobus solfataricus with as ligand. Known structural/functional Sites: , , , , , and . Full crystallographic information is available from OCA.
Reference
Structure of the DNA repair helicase hel308 reveals DNA binding and autoinhibitory domains., Richards JD, Johnson KA, Liu H, McRobbie AM, McMahon S, Oke M, Carter L, Naismith JH, White MF, J Biol Chem. 2008 Feb 22;283(8):5118-26. Epub 2007 Dec 4. PMID:18056710
Page seeded by OCA on Thu Feb 21 18:54:31 2008
Categories: Single protein | Sulfolobus solfataricus | Carter, L. | Johnson, K A. | Liu, H. | Mcmahon, S. | Naismith, J H. | Oke, M. | Richards, J. | White, M F. | SO4 | Atp-binding | Dna repair | Hel308 | Helicase | Hydrolase | Nucleotide-binding | Sso2462
