2ok2
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The Escherichia coli mispair-binding protein MutS forms dimers and | + | 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== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Escherichia coli MutS | + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17426027 17426027] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Kolodner, R | + | [[Category: Kolodner, R D.]] |
| - | [[Category: Mendillo, M | + | [[Category: Mendillo, M L.]] |
| - | [[Category: Putnam, C | + | [[Category: Putnam, C D.]] |
[[Category: MAL]] | [[Category: MAL]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: tetramerization]] | [[Category: tetramerization]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:19:22 2008'' |
Revision as of 16:19, 21 February 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
Page seeded by OCA on Thu Feb 21 18:19:22 2008
