1e3m

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(New page: 200px<br /><applet load="1e3m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e3m, resolution 2.2&Aring;" /> '''THE CRYSTAL STRUCTURE...)
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'''THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A G:T MISMATCH'''<br />
'''THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A G:T MISMATCH'''<br />
==Overview==
==Overview==
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DNA mismatch repair ensures genomic integrity on DNA replication., Recognition of a DNA mismatch by a dimeric MutS protein initiates a, cascade of reactions and results in repair of the newly synthesized, strand; however, details of the molecular mechanism remain controversial., Here we present the crystal structure at 2.2 A of MutS from Escherichia, coli bound to a G x T mismatch. The two MutS monomers have different, conformations and form a heterodimer at the structural level. Only one, monomer recognizes the mismatch specifically and has ADP bound. Mismatch, recognition occurs by extensive minor groove interactions causing unusual, base pairing and kinking of the DNA. Nonspecific major groove DNA-binding, domains from both monomers embrace the DNA in a clamp-like structure. The, interleaved nucleotide-binding sites are located far from the DNA., Mutations in human MutS alpha (MSH2/MSH6) that lead to hereditary, predisposition for cancer, such as hereditary non-polyposis colorectal, cancer, can be mapped to this crystal structure.
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DNA mismatch repair ensures genomic integrity on DNA replication. Recognition of a DNA mismatch by a dimeric MutS protein initiates a cascade of reactions and results in repair of the newly synthesized strand; however, details of the molecular mechanism remain controversial. Here we present the crystal structure at 2.2 A of MutS from Escherichia coli bound to a G x T mismatch. The two MutS monomers have different conformations and form a heterodimer at the structural level. Only one monomer recognizes the mismatch specifically and has ADP bound. Mismatch recognition occurs by extensive minor groove interactions causing unusual base pairing and kinking of the DNA. Nonspecific major groove DNA-binding domains from both monomers embrace the DNA in a clamp-like structure. The interleaved nucleotide-binding sites are located far from the DNA. Mutations in human MutS alpha (MSH2/MSH6) that lead to hereditary predisposition for cancer, such as hereditary non-polyposis colorectal cancer, can be mapped to this crystal structure.
==About this Structure==
==About this Structure==
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1E3M 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 MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E3M OCA].
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1E3M 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=MG:'>MG</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=1E3M OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Enzlin, J.]]
[[Category: Enzlin, J.]]
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[[Category: Lamers, M.H.]]
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[[Category: Lamers, M H.]]
[[Category: Perrakis, A.]]
[[Category: Perrakis, A.]]
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[[Category: Sixma, T.K.]]
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[[Category: Sixma, T K.]]
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[[Category: Wind, N.De.]]
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[[Category: Wind, N De.]]
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[[Category: Winterwerp, H.H.K.]]
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[[Category: Winterwerp, H H.K.]]
[[Category: ADP]]
[[Category: ADP]]
[[Category: MG]]
[[Category: MG]]
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[[Category: mismatch recognition]]
[[Category: mismatch recognition]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:45:41 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:23:24 2008''

Revision as of 10:23, 21 February 2008


1e3m, resolution 2.2Å

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THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A G:T MISMATCH

Overview

DNA mismatch repair ensures genomic integrity on DNA replication. Recognition of a DNA mismatch by a dimeric MutS protein initiates a cascade of reactions and results in repair of the newly synthesized strand; however, details of the molecular mechanism remain controversial. Here we present the crystal structure at 2.2 A of MutS from Escherichia coli bound to a G x T mismatch. The two MutS monomers have different conformations and form a heterodimer at the structural level. Only one monomer recognizes the mismatch specifically and has ADP bound. Mismatch recognition occurs by extensive minor groove interactions causing unusual base pairing and kinking of the DNA. Nonspecific major groove DNA-binding domains from both monomers embrace the DNA in a clamp-like structure. The interleaved nucleotide-binding sites are located far from the DNA. Mutations in human MutS alpha (MSH2/MSH6) that lead to hereditary predisposition for cancer, such as hereditary non-polyposis colorectal cancer, can be mapped to this crystal structure.

About this Structure

1E3M is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

Reference

The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch., Lamers MH, Perrakis A, Enzlin JH, Winterwerp HH, de Wind N, Sixma TK, Nature. 2000 Oct 12;407(6805):711-7. PMID:11048711

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