TY - JOUR
T1 - Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase
AU - Sharma, Vivek
AU - Arockiasamy, Arulandu
AU - Ronning, Donald R.
AU - Savva, Christos G.
AU - Holzenburg, Andreas
AU - Braunstein, Miriam
AU - Jacobs, William R.
AU - Sacchettini, James C.
PY - 2003/3/4
Y1 - 2003/3/4
N2 - In bacteria, the majority of exported proteins are translocated by the Sec system, which recognizes the signal sequence of a preprotein and uses ATP and the proton motive force to mediate protein translocation across the cytoplasmic membrane. SecA is an essential protein component of this system, containing the molecular motor that facilitates translocation. Here we report the threedimensional structure of the SecA protein of Mycobacterium tuberculosis. Each subunit of the homodimer contains a "motor" domain and a translocation domain. The structure predicts that SecA can interact with the SecYEG pore and function as a molecular ratchet that uses ATP hydrolysis for physical movement of the preprotein. Knowledge of this structure provides a framework for further elucidation of the translocation process.
AB - In bacteria, the majority of exported proteins are translocated by the Sec system, which recognizes the signal sequence of a preprotein and uses ATP and the proton motive force to mediate protein translocation across the cytoplasmic membrane. SecA is an essential protein component of this system, containing the molecular motor that facilitates translocation. Here we report the threedimensional structure of the SecA protein of Mycobacterium tuberculosis. Each subunit of the homodimer contains a "motor" domain and a translocation domain. The structure predicts that SecA can interact with the SecYEG pore and function as a molecular ratchet that uses ATP hydrolysis for physical movement of the preprotein. Knowledge of this structure provides a framework for further elucidation of the translocation process.
UR - http://www.scopus.com/inward/record.url?scp=0345184333&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0345184333&partnerID=8YFLogxK
U2 - 10.1073/pnas.0538077100
DO - 10.1073/pnas.0538077100
M3 - Article
C2 - 12606717
AN - SCOPUS:0345184333
SN - 0027-8424
VL - 100
SP - 2243
EP - 2248
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 5
ER -