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| | {{STRUCTURE_2va8| PDB=2va8 | SCENE= }} | | {{STRUCTURE_2va8| PDB=2va8 | SCENE= }} |
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| - | '''DNA REPAIR HELICASE HEL308'''
| + | ===DNA REPAIR HELICASE HEL308=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_18056710}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 18056710 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_18056710}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Nucleotide-binding]] | | [[Category: Nucleotide-binding]] |
| | [[Category: Sso2462]] | | [[Category: Sso2462]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:28:49 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:36:34 2008'' |
Revision as of 13:36, 28 July 2008
Template:STRUCTURE 2va8
DNA REPAIR HELICASE HEL308
Template:ABSTRACT PUBMED 18056710
About this Structure
2VA8 is a Single protein structure of sequence from Sulfolobus solfataricus. 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 Mon Jul 28 16:36:34 2008
