1ewq
From Proteopedia
(New page: 200px<br /><applet load="1ewq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ewq, resolution 2.20Å" /> '''CRYSTAL STRUCTURE TA...) |
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| - | [[Image:1ewq.gif|left|200px]]<br /><applet load="1ewq" size=" | + | [[Image:1ewq.gif|left|200px]]<br /><applet load="1ewq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ewq, resolution 2.20Å" /> | caption="1ewq, resolution 2.20Å" /> | ||
'''CRYSTAL STRUCTURE TAQ MUTS COMPLEXED WITH A HETERODUPLEX DNA AT 2.2 A RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE TAQ MUTS COMPLEXED WITH A HETERODUPLEX DNA AT 2.2 A RESOLUTION'''<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== | ||
| - | 1EWQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with SO4 and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1EWQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EWQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: one domain is entirely helical]] | [[Category: one domain is entirely helical]] | ||
| - | ''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 TAQ MUTS COMPLEXED WITH A HETERODUPLEX DNA AT 2.2 A RESOLUTION
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
1EWQ is a Single protein structure of sequence from Thermus aquaticus with and as ligands. 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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