1ewr
From Proteopedia
(New page: 200px<br /><applet load="1ewr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ewr, resolution 3.19Å" /> '''CRYSTAL STRUCTURE OF...) |
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- | [[Image:1ewr.gif|left|200px]]<br /><applet load="1ewr" size=" | + | [[Image:1ewr.gif|left|200px]]<br /><applet load="1ewr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ewr, resolution 3.19Å" /> | caption="1ewr, resolution 3.19Å" /> | ||
'''CRYSTAL STRUCTURE OF TAQ MUTS'''<br /> | '''CRYSTAL STRUCTURE OF TAQ MUTS'''<br /> | ||
==Overview== | ==Overview== | ||
- | DNA mismatch repair is critical for increasing replication fidelity in | + | 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== | ==About this Structure== | ||
- | 1EWR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http:// | + | 1EWR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EWR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: dna-binding]] | [[Category: dna-binding]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:17 2008'' |
Revision as of 10:32, 21 February 2008
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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
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