Overall Shapes of the SMC-ScpAB Complex Are Determined by Balance between Constraint and Relaxation of Its Structural Parts

Structure

Volumn 25, Issue 4, 2017, Pages 603-616.e4

  Kamada, Katsuhiko ^a   Su'etsugu, Masayuki ^b   Takada, Hiraku ^b   Miyata, Makoto ^c   Hirano, Tatsuya ^a  

^a RIKEN   (Japan)

^b RIKKYO UNIVERSITY   (Japan)

^c Osaka Prefecture University   (Japan)

Author keywords

ATPase; Bacillus subtilis; chromosome organization; Condensin; ScpA; ScpB; segregation; SMC

Indexed keywords

ADENOSINE TRIPHOSPHATE; MULTIPROTEIN COMPLEX; SMC SCPAB COMPLEX; UNCLASSIFIED DRUG; CELL CYCLE PROTEIN; PROTEIN BINDING;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN STRUCTURE; BINDING SITE; CHEMISTRY; GENETICS; METABOLISM; MOLECULAR MODEL; PROTEIN MULTIMERIZATION; X RAY CRYSTALLOGRAPHY;

BINDING SITES; CELL CYCLE PROTEINS; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; MUTATION; PROTEIN BINDING; PROTEIN MULTIMERIZATION;

EID: 85014599850     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2017.02.008     Document Type: Article

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