Crystal structure and biochemical analysis of the MutS.ADP.beryllium fluoride complex suggests a conserved mechanism for ATP interactions in mismatch repair (Q27640487)

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scientific article (publication date: 2 May 2003)

Language	Label	Description	Also known as
English	Crystal structure and biochemical analysis of the MutS.ADP.beryllium fluoride complex suggests a conserved mechanism for ATP interactions in mismatch repair	scientific article (publication date: 2 May 2003)

Statements

scholarly article

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Crystal structure and biochemical analysis of the MutS.ADP.beryllium fluoride complex suggests a conserved mechanism for ATP interactions in mismatch repair (English)

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crystal structure

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DNA mismatch repair

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based on heuristic

inferred from title

author name string

Eric Alani

1

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Jae Young Lee

2

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Mark J Schofield

3

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Amanda W Kijas

4

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Peggy Hsieh

5

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Wei Yang

6

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language of work or name

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publication date

2 May 2003

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Journal of Biological Chemistry

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278

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18

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16088-94

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Mismatch repair in replication fidelity, genetic recombination, and cancer biology

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Evidence for a physical interaction between the Escherichia coli methyl-directed mismatch repair proteins MutL and UvrD.

1 reference

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Mismatch-, MutS-, MutL-, and helicase II-dependent unwinding from the single-strand break of an incised heteroduplex

1 reference

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MutS and MutL activate DNA helicase II in a mismatch-dependent manner

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Escherichia coli MutL loads DNA helicase II onto DNA.

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Eukaryotic DNA mismatch repair

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DNA mismatch repair and mutation avoidance pathways

1 reference

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Enhancement of MSH2-MSH3-mediated mismatch recognition by the yeast MLH1-PMS1 complex

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ATP-dependent assembly of a ternary complex consisting of a DNA mismatch and the yeast MSH2-MSH6 and MLH1-PMS1 protein complexes

1 reference

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Evidence for involvement of yeast proliferating cell nuclear antigen in DNA mismatch repair

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https://api.crossref.org/works/10.1074%2FJBC.M213193200

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Requirement for PCNA in DNA mismatch repair at a step preceding DNA resynthesis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

21 January 2018

ATP-dependent interaction of human mismatch repair proteins and dual role of PCNA in mismatch repair

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

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Functional interaction of proliferating cell nuclear antigen with MSH2-MSH6 and MSH2-MSH3 complexes

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Proliferating cell nuclear antigen and Msh2p-Msh6p interact to form an active mispair recognition complex

1 reference

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hMSH3 and hMSH6 interact with PCNA and colocalize with it to replication foci

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

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MSH-MLH complexes formed at a DNA mismatch are disrupted by the PCNA sliding clamp

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

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Transfer of the MSH2.MSH6 complex from proliferating cell nuclear antigen to mispaired bases in DNA.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

21 January 2018

MutS mediates heteroduplex loop formation by a translocation mechanism

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https://api.crossref.org/works/10.1074%2FJBC.M213193200

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DNA-dependent activation of the hMutSalpha ATPase

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https://api.crossref.org/works/10.1074%2FJBC.M213193200

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The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch

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https://api.crossref.org/works/10.1074%2FJBC.M213193200

21 January 2018

The role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular switch

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https://api.crossref.org/works/10.1074%2FJBC.M213193200

21 January 2018

Composite active site of an ABC ATPase: MutS uses ATP to verify mismatch recognition and authorize DNA repair

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

21 January 2018

Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

21 January 2018

The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

21 January 2018

The Saccharomyces cerevisiae Msh2 and Msh6 proteins form a complex that specifically binds to duplex oligonucleotides containing mismatched DNA base pairs

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

21 January 2018

Purification of eukaryotic MutL homologs from Saccharomyces cerevisiae using self-affinity technology.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

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Chemistry and biology

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https://api.crossref.org/works/10.1074%2FJBC.M213193200

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Processing of X-ray diffraction data collected in oscillation mode

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

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Analysis of yeast MSH2-MSH6 suggests that the initiation of mismatch repair can be separated into discrete steps

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

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X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

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Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein and its complex with tungstate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

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Vanadate inhibits the ATPase activity and DNA binding capability of bacterial MutS. A structural model for the vanadate-MutS interaction at the Walker A motif

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

21 January 2018

Saccharomyces cerevisiae Msh2p and Msh6p ATPase activities are both required during mismatch repair

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

21 January 2018

hMSH2 and hMSH6 play distinct roles in mismatch binding and contribute differently to the ATPase activity of hMutSalpha

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

21 January 2018

3D domain swapping: as domains continue to swap

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

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Conserved domains in DNA repair proteins and evolution of repair systems

1 reference

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Subunit interactions in ABC transporters: towards a functional architecture

1 reference

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Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

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RAD50 protein of S.cerevisiae exhibits ATP-dependent DNA binding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

21 January 2018

Disruption of the helix-u-turn-helix motif of MutS protein: loss of subunit dimerization, mismatch binding and ATP hydrolysis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M213193200

21 January 2018

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10.1074/JBC.M213193200

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