1fw6: Difference between revisions
New page: left|200px<br /><applet load="1fw6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fw6, resolution 2.70Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1fw6.gif|left|200px]]<br /><applet load="1fw6" size=" | [[Image:1fw6.gif|left|200px]]<br /><applet load="1fw6" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1fw6, resolution 2.70Å" /> | caption="1fw6, resolution 2.70Å" /> | ||
'''CRYSTAL STRUCTURE OF A TAQ MUTS-DNA-ADP TERNARY COMPLEX'''<br /> | '''CRYSTAL STRUCTURE OF A TAQ MUTS-DNA-ADP TERNARY COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
The MutS protein initiates DNA mismatch repair by recognizing mispaired | The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. Here we report the crystal structure of a ternary complex of MutS-DNA-ADP and assays of initiation of mismatch repair in conjunction with perturbation of the composite ATPase active site by mutagenesis. These studies indicate that MutS has to bind both ATP and the mismatch DNA simultaneously in order to activate the other mismatch repair proteins. We propose that the MutS ATPase activity plays a proofreading role in DNA mismatch repair, verification of mismatch recognition, and authorization of repair. | ||
==About this Structure== | ==About this Structure== | ||
1FW6 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 MG, SO4 and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1FW6 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=MG:'>MG</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FW6 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Thermus aquaticus]] | [[Category: Thermus aquaticus]] | ||
[[Category: Hsieh, P.]] | [[Category: Hsieh, P.]] | ||
[[Category: Junop, M | [[Category: Junop, M S.]] | ||
[[Category: Obmolova, G.]] | [[Category: Obmolova, G.]] | ||
[[Category: Rausch, K.]] | [[Category: Rausch, K.]] | ||
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[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:25 2008'' | ||
Revision as of 13:43, 21 February 2008
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CRYSTAL STRUCTURE OF A TAQ MUTS-DNA-ADP TERNARY COMPLEX
OverviewOverview
The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. Here we report the crystal structure of a ternary complex of MutS-DNA-ADP and assays of initiation of mismatch repair in conjunction with perturbation of the composite ATPase active site by mutagenesis. These studies indicate that MutS has to bind both ATP and the mismatch DNA simultaneously in order to activate the other mismatch repair proteins. We propose that the MutS ATPase activity plays a proofreading role in DNA mismatch repair, verification of mismatch recognition, and authorization of repair.
About this StructureAbout this Structure
1FW6 is a Single protein structure of sequence from Thermus aquaticus with , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Composite active site of an ABC ATPase: MutS uses ATP to verify mismatch recognition and authorize DNA repair., Junop MS, Obmolova G, Rausch K, Hsieh P, Yang W, Mol Cell. 2001 Jan;7(1):1-12. PMID:11172706
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