1ewr
From Proteopedia
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'''CRYSTAL STRUCTURE OF TAQ MUTS''' | '''CRYSTAL STRUCTURE OF TAQ MUTS''' | ||
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[[Category: Obmolova, G.]] | [[Category: Obmolova, G.]] | ||
[[Category: Yang, W.]] | [[Category: Yang, W.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:36:35 2008'' | |
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Revision as of 12:36, 2 May 2008
CRYSTAL STRUCTURE OF TAQ MUTS
Overview
DNA mismatch repair is critical for increasing replication fidelity in organisms ranging from bacteria to humans. MutS protein, a member of the ABC ATPase superfamily, recognizes mispaired and unpaired bases in duplex DNA and initiates mismatch repair. Mutations in human MutS genes cause a predisposition to hereditary nonpolyposis colorectal cancer as well as sporadic tumours. Here we report the crystal structures of a MutS protein and a complex of MutS with a heteroduplex DNA containing an unpaired base. The structures reveal the general architecture of members of the MutS family, an induced-fit mechanism of recognition between four domains of a MutS dimer and a heteroduplex kinked at the mismatch, a composite ATPase active site composed of residues from both MutS subunits, and a transmitter region connecting the mismatch-binding and ATPase domains. The crystal structures also provide a molecular framework for understanding hereditary nonpolyposis colorectal cancer mutations and for postulating testable roles of MutS.
About this Structure
1EWR is a Single protein structure of sequence from Thermus aquaticus. Full crystallographic information is available from OCA.
Reference
Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA., Obmolova G, Ban C, Hsieh P, Yang W, Nature. 2000 Oct 12;407(6805):703-10. PMID:11048710 Page seeded by OCA on Fri May 2 15:36:35 2008
