PvuII endonuclease contains two calcium ions in active sites
about
Structure and function of type II restriction endonucleasesInference of relationships in the 'twilight zone' of homology using a combination of bioinformatics and site-directed mutagenesis: a case study of restriction endonucleases Bsp6I and PvuIIStructure of HinP1I endonuclease reveals a striking similarity to the monomeric restriction enzyme MspI.Developing a programmed restriction endonuclease for highly specific DNA cleavageThe crystal structure of sphingosine-1-phosphate in complex with a Fab fragment reveals metal bridging of an antibody and its antigenNew clues in the allosteric activation of DNA cleavage bySgrAI: structures ofSgrAI bound to cleaved primary-site DNA and uncleaved secondary-site DNACrystal structure and mechanism of action of the N6-methyladenine-dependent type IIM restriction endonuclease R.DpnIStructural basis of the methylation specificity of R.DpnIProtein stability indicates divergent evolution of PD-(D/E)XK type II restriction endonucleases.PrfA protein of Bacillus species: prediction and demonstration of endonuclease activity on DNAThe use of divalent metal ions by type II topoisomerases.Cooperation and competition in mismatch repair: very short-patch repair and methyl-directed mismatch repair in Escherichia coli.Mobility of a restriction-modification system revealed by its genetic contexts in three hosts.Now on display: a gallery of group II intron structures at different stages of catalysisESR spectroscopy identifies inhibitory Cu2+ sites in a DNA-modifying enzyme to reveal determinants of catalytic specificityHuman topoisomerase IIalpha uses a two-metal-ion mechanism for DNA cleavage.Kinetic analysis of product release and metal ions in a metallonuclease.Analysis of the HindIII-catalyzed reaction by time-resolved crystallographyA novel zinc-finger nuclease platform with a sequence-specific cleavage module.Nucleophile activation in PD...(D/E)xK metallonucleases: an experimental and computational pK(a) study.One- and two-metal ion catalysis: global single-turnover kinetic analysis of the PvuII endonuclease mechanism.Ca(2+)-mediated site-specific DNA cleavage and suppression of promiscuous activity of KpnI restriction endonuclease.Clustering biomolecular complexes by residue contacts similarity.
P2860
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P2860
PvuII endonuclease contains two calcium ions in active sites
description
2000 nî lūn-bûn
@nan
2000 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
PvuII endonuclease contains two calcium ions in active sites
@ast
PvuII endonuclease contains two calcium ions in active sites
@en
PvuII endonuclease contains two calcium ions in active sites
@nl
type
label
PvuII endonuclease contains two calcium ions in active sites
@ast
PvuII endonuclease contains two calcium ions in active sites
@en
PvuII endonuclease contains two calcium ions in active sites
@nl
prefLabel
PvuII endonuclease contains two calcium ions in active sites
@ast
PvuII endonuclease contains two calcium ions in active sites
@en
PvuII endonuclease contains two calcium ions in active sites
@nl
P356
P1476
PvuII endonuclease contains two calcium ions in active sites
@en
P2093
P304
P356
10.1006/JMBI.2000.3938
P407
P577
2000-07-01T00:00:00Z