Mycobacterium tuberculosis FtsX extracellular domain activates the peptidoglycan hydrolase, RipC

Proceedings of the National Academy of Sciences of the United States of America

Volumn 111, Issue 22, 2014, Pages 8037-8042

  Mavrici, Daniela ^a   Marakalala, Mohlopheni J ^b   Holton, James M ^c,d   Prigozhin, Daniil M ^a   Gee, Christine L ^e   Zhang, Yanjia J ^b   Rubin, Eric J ^b   Alber, Tom ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b HARVARD SCHOOL OF PUBLIC HEALTH   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^e AUSTRALIAN SYNCHROTRON   (Australia)

Author keywords

Bacterial cell wall; Divisome; Extracellular signaling; Long range conformational change

Indexed keywords

FTSX EXTRACELLULAR DOMAIN; HYDROLASE; MEMBRANE PROTEIN; PEPTIDOGLYCAN; RIPC; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL CELL; BACTERIAL GROWTH; BINDING SITE; CELL DIVISION; CELL WALL; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DAUGHTER CELL; GENETIC ANALYSIS; HYDROPHOBICITY; IN VITRO STUDY; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN HYDROLYSIS;

BACTERIAL CELL WALL; DIVISOME; EXTRACELLULAR SIGNALING; LONG-RANGE CONFORMATIONAL CHANGE;

AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BINDING SITES; CELL CYCLE PROTEINS; CELL WALL; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; HYDROLYSIS; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; PHENOTYPE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SIGNAL TRANSDUCTION; VIRULENCE FACTORS;

EID: 84901818376     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1321812111     Document Type: Article

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