NMR characterization of the interaction of the endonuclease domain of MutL with divalent metal ions and ATP

PLoS ONE

Volumn 9, Issue 6, 2014, Pages

  Mizushima, Ryota ^a   Kim, Ju Yaen ^a   Suetake, Isao ^a   Tanaka, Hiroaki ^a   Takai, Tomoyo ^a   Kamiya, Narutoshi ^a   Takano, Yu ^a   Mishima, Yuichi ^a   Tajima, Shoji ^a   Goto, Yuji ^a   Fukui, Kenji ^b,c   Lee, Young Ho ^a  

^a OSAKA UNIVERSITY   (Japan)

^b RIKEN SPring 8 Center   (Japan)

^c TransGenic Inc Kobe Research Center   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ENDONUCLEASE; MANGANESE; METAL ION; PROTEIN MUTL; ZINC ION; ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; ION; METAL; PROTEIN BINDING; SOLUTION AND SOLUBILITY;

AMINO TERMINAL SEQUENCE; AQUIFEX AEOLICUS; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME REGULATION; ENZYME STABILITY; MISMATCH REPAIR; MOLECULAR DOCKING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN DNA INTERACTION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN NUCLEIC ACID INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; CONFORMATION; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PROTEIN STABILITY; SOLUTION AND SOLUBILITY; THERMODYNAMICS;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEINS; BINDING SITES; ENDONUCLEASES; IONS; METALS; MODELS, MOLECULAR; MOLECULAR CONFORMATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STABILITY; SOLUTIONS; THERMODYNAMICS;

EID: 84902436685     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0098554     Document Type: Article

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