2rhf
From Proteopedia
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'''D. radiodurans RecQ HRDC domain 3''' | '''D. radiodurans RecQ HRDC domain 3''' | ||
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| + | ==Overview== | ||
| + | RecQ helicases are critical for maintaining genome integrity in organisms ranging from bacteria to humans by participating in a complex network of DNA metabolic pathways. Their diverse cellular functions require specialization and coordination of multiple protein domains that integrate catalytic functions with DNA-protein and protein-protein interactions. The RecQ helicase from Deinococcus radiodurans (DrRecQ) is unusual among RecQ family members in that it has evolved to utilize three 'Helicase and RNaseD C-terminal' (HRDC) domains to regulate its activity. In this report, we describe the high-resolution structure of the C-terminal-most HRDC domain of DrRecQ. The structure reveals unusual electrostatic surface features that distinguish it from other HRDC domains. Mutation of individual residues in these regions affects the DNA binding affinity of DrRecQ and its ability to unwind a partial duplex DNA substrate. Taken together, the results suggest the unusual electrostatic surface features of the DrRecQ HRDC domain may be important for inter-domain interactions that regulate structure-specific DNA binding and help direct DrRecQ to specific recombination/repair sites. | ||
==About this Structure== | ==About this Structure== | ||
| - | 2RHF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 2RHF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans_r1 Deinococcus radiodurans r1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RHF OCA]. |
| - | [[Category: Deinococcus radiodurans]] | + | |
| + | ==Reference== | ||
| + | Structure and function of the regulatory C-terminal HRDC domain from Deinococcus radiodurans RecQ., Killoran MP, Keck JL, Nucleic Acids Res. 2008 May;36(9):3139-49. Epub 2008 Apr 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18411208 18411208] | ||
| + | [[Category: Deinococcus radiodurans r1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Keck, J L.]] | [[Category: Keck, J L.]] | ||
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[[Category: Nucleotide-binding]] | [[Category: Nucleotide-binding]] | ||
[[Category: Recq]] | [[Category: Recq]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 4 09:59:13 2008'' |
Revision as of 06:59, 4 June 2008
D. radiodurans RecQ HRDC domain 3
Overview
RecQ helicases are critical for maintaining genome integrity in organisms ranging from bacteria to humans by participating in a complex network of DNA metabolic pathways. Their diverse cellular functions require specialization and coordination of multiple protein domains that integrate catalytic functions with DNA-protein and protein-protein interactions. The RecQ helicase from Deinococcus radiodurans (DrRecQ) is unusual among RecQ family members in that it has evolved to utilize three 'Helicase and RNaseD C-terminal' (HRDC) domains to regulate its activity. In this report, we describe the high-resolution structure of the C-terminal-most HRDC domain of DrRecQ. The structure reveals unusual electrostatic surface features that distinguish it from other HRDC domains. Mutation of individual residues in these regions affects the DNA binding affinity of DrRecQ and its ability to unwind a partial duplex DNA substrate. Taken together, the results suggest the unusual electrostatic surface features of the DrRecQ HRDC domain may be important for inter-domain interactions that regulate structure-specific DNA binding and help direct DrRecQ to specific recombination/repair sites.
About this Structure
2RHF is a Single protein structure of sequence from Deinococcus radiodurans r1. Full crystallographic information is available from OCA.
Reference
Structure and function of the regulatory C-terminal HRDC domain from Deinococcus radiodurans RecQ., Killoran MP, Keck JL, Nucleic Acids Res. 2008 May;36(9):3139-49. Epub 2008 Apr 13. PMID:18411208 Page seeded by OCA on Wed Jun 4 09:59:13 2008
