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1ewq

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[[Image:1ewq.gif|left|200px]]<br /><applet load="1ewq" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ewq.gif|left|200px]]
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caption="1ewq, resolution 2.20&Aring;" />
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'''CRYSTAL STRUCTURE TAQ MUTS COMPLEXED WITH A HETERODUPLEX DNA AT 2.2 A RESOLUTION'''<br />
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{{Structure
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|PDB= 1ewq |SIZE=350|CAPTION= <scene name='initialview01'>1ewq</scene>, resolution 2.20&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURE TAQ MUTS COMPLEXED WITH A HETERODUPLEX DNA AT 2.2 A RESOLUTION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1EWQ is a [[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=1EWQ OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11048710 11048710]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11048710 11048710]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermus aquaticus]]
[[Category: Thermus aquaticus]]
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[[Category: SO4]]
[[Category: SO4]]
[[Category: double stranded helix]]
[[Category: double stranded helix]]
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[[Category: mostly mixed alpha-beta structures]]
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[[Category: mostly mixed alpha-beta structure]]
[[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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:01:15 2008''

Revision as of 09:01, 20 March 2008


PDB ID 1ewq

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



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. 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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