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Crystallographic and functional studies of very short patch repair endonuclease
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title
Crystallographic and functional studies of very short patch repair endonuclease
(English)
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author
Susan E Tsutakawa
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stated in
ORCID Public Data File 2021
author name string
S E Tsutakawa
series ordinal
1
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T Muto
series ordinal
2
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T Kawate
series ordinal
3
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H Jingami
series ordinal
4
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N Kunishima
series ordinal
5
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M Ariyoshi
series ordinal
6
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D Kohda
series ordinal
7
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M Nakagawa
series ordinal
8
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K Morikawa
series ordinal
9
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publication date
May 1999
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published in
Molecular Cell
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volume
3
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page(s)
621-8
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issue
5
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cites work
Structure and function of restriction endonucleases
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MutS mediates heteroduplex loop formation by a translocation mechanism
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Crystal structure of PvuII endonuclease reveals extensive structural homologies to EcoRV
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Structural basis for MutH activation in E.coli mismatch repair and relationship of MutH to restriction endonucleases
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Crystal structure of Citrobacter freundii restriction endonuclease Cfr10I at 2.15 A resolution
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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
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The CCP4 suite: programs for protein crystallography
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Crystal structure of the PvuII restriction endonuclease
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Identification of the XorII methyltransferase gene and a vsr homolog from Xanthomonas oryzae pv. oryzae
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Molecular basis of base substitution hotspots in Escherichia coli
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The Escherichia coli MutL protein stimulates binding of Vsr and MutS to heteroduplex DNA.
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Genetic requirements for hyper-recombination by very short patch mismatch repair: involvement of Escherichia coli DNA polymerase I.
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DNA binding and cleavage by the nuclear intron-encoded homing endonuclease I-PpoI
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Substrate preferences of Vsr DNA mismatch endonuclease and their consequences for the evolution of the Escherichia coli K-12 genome.
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Does the Restriction EndonucleaseEcoRV Employ a Two-Metal-Ion Mechanism for DNA Cleavage?†
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The importance of not saturating water in protein NMR. Application to sensitivity enhancement and NOE measurements
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Nucleotide sequence of the dcm locus of Escherichia coli K12.
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The vsr gene product of E. coli K-12 is a strand- and sequence-specific DNA mismatch endonuclease
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Metal ion-mediated substrate-assisted catalysis in type II restriction endonucleases
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Mismatch repair of deaminated 5-methyl-cytosine.
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Mg2+ binding to the active site of EcoRV endonuclease: a crystallographic study of complexes with substrate and product DNA at 2 A resolution
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Organization and sequence of the HpaII restriction-modification system and adjacent genes.
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Bacterial genes mutL, mutS, and dcm participate in repair of mismatches at 5-methylcytosine sites
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Identifiers
DOI
10.1016/S1097-2765(00)80355-X
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PubMed ID
10360178
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