1ewq: Difference between revisions

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[[Image:1ewq.gif|left|200px]]
{{Seed}}
[[Image:1ewq.png|left|200px]]


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{{STRUCTURE_1ewq|  PDB=1ewq  |  SCENE=  }}  
{{STRUCTURE_1ewq|  PDB=1ewq  |  SCENE=  }}  


'''CRYSTAL STRUCTURE TAQ MUTS COMPLEXED WITH A HETERODUPLEX DNA AT 2.2 A RESOLUTION'''
===CRYSTAL STRUCTURE TAQ MUTS COMPLEXED WITH A HETERODUPLEX DNA AT 2.2 A RESOLUTION===




==Overview==
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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.
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{{ABSTRACT_PUBMED_11048710}}


==About this Structure==
==About this Structure==
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[[Category: Multiple domains of protein]]
[[Category: Multiple domains of protein]]
[[Category: One domain is entirely helical]]
[[Category: One domain is entirely helical]]
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