2ok2
From Proteopedia
(New page: 200px<br /><applet load="2ok2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ok2, resolution 2.00Å" /> '''MutS C-terminal doma...) |
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| - | [[Image:2ok2.gif|left|200px]]<br /><applet load="2ok2" size=" | + | [[Image:2ok2.gif|left|200px]]<br /><applet load="2ok2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ok2, resolution 2.00Å" /> | caption="2ok2, resolution 2.00Å" /> | ||
'''MutS C-terminal domain fused to Maltose Binding Protein'''<br /> | '''MutS C-terminal domain fused to Maltose Binding Protein'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2OK2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MAL and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2OK2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MAL:'>MAL</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OK2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tetramerization]] | [[Category: tetramerization]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:53:28 2008'' |
Revision as of 12:53, 23 January 2008
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MutS C-terminal domain fused to Maltose Binding Protein
Overview
The Escherichia coli mispair-binding protein MutS forms dimers and, tetramers in vitro, although the functional form in vivo is under debate., Here we demonstrate that the MutS tetramer is extended in solution using, small angle x-ray scattering and the crystal structure of the C-terminal, 34 amino acids of MutS containing the tetramer-forming domain fused to, maltose-binding protein (MBP). Wild-type C-terminal MBP fusions formed, tetramers and could bind MutS and MutS-MutL-DNA complexes. In contrast, D835R and R840E mutations predicted to disrupt tetrameric interactions, only allowed dimerization of MBP. A chromosomal MutS truncation mutation, eliminating the dimerization/tetramerization domain eliminated mismatch, repair, whereas the tetramer-disrupting MutS D835R and R840E mutations, only modestly affected MutS function. These results demonstrate that, dimerization but not tetramerization of the MutS C terminus is essential, for mismatch repair.
About this Structure
2OK2 is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
Reference
Escherichia coli MutS Tetramerization Domain Structure Reveals That Stable Dimers but Not Tetramers Are Essential for DNA Mismatch Repair in Vivo., Mendillo ML, Putnam CD, Kolodner RD, J Biol Chem. 2007 Jun 1;282(22):16345-54. Epub 2007 Apr 10. PMID:17426027
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