Large lateral movement of transmembrane helix S5 is not required for substrate access to the active site of rhomboid intramembrane protease

Journal of Biological Chemistry

Volumn 288, Issue 23, 2013, Pages 16645-16654

  Xue, Yi ^a   Ha, Ya ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COCRYSTAL STRUCTURE; CONFORMATIONAL CHANGE; DETERGENT SOLUTION; MEMBRANE PROTEINS; MEMBRANE VESICLES; POLYTOPIC MEMBRANE PROTEINS; TRANS-MEMBRANE PROTEINS; TRANSMEMBRANE HELICES;

BIOLOGICAL MEMBRANES;

SUBSTRATES;

GLPG PROTEIN; PROTEINASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; PRIORITY JOURNAL; PROTEIN CROSS LINKING; S5 HELIX;

ENZYME MECHANISMS; INTRAMEMBRANE PROTEOLYSIS; PROTEIN CONFORMATION; RHOMBOID PROTEASE; X-RAY CRYSTALLOGRAPHY;

CATALYTIC DOMAIN; CELL MEMBRANE; CRYSTALLOGRAPHY, X-RAY; DNA-BINDING PROTEINS; ENDOPEPTIDASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MEMBRANE PROTEINS; PROTEIN STRUCTURE, SECONDARY;

BACTERIA (MICROORGANISMS);

EID: 84878409837     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.438127     Document Type: Article

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