1NL3

CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS in APO FORM

Summary for 1NL3

• Entry DOI: 10.2210/pdb1nl3/pdb
• Related: 1NKT
• Descriptor: PREPROTEIN TRANSLOCASE SECA 1 SUBUNIT (2 entities in total)
• Functional Keywords: preprotein translocation, atpase, transmembrane transport, helicase-like motor domain, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, protein transport
• Biological source: Mycobacterium tuberculosis
• Cellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P0A5Y8
• Total number of polymer chains: 2
• Total formula weight: 206927.75

Authors

Sharma, V.,Arockiasamy, A.,Ronning, D.R.,Savva, C.G.,Holzenburg, A.,Braunstein, M.,Jacobs Jr., W.R.,Sacchettini, J.C.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2003-01-06, release date: 2003-03-04, Last modification date: 2024-02-14)

Primary citation

Sharma, V.,Arockiasamy, A.,Ronning, D.R.,Savva, C.G.,Holzenburg, A.,Braunstein, M.,Jacobs Jr., W.R.,Sacchettini, J.C.
Crystal Structure of M. tuberculosis SecA, A Preprotein Translocating ATPase
Proc.Natl.Acad.Sci.USA, 100:2243-2248, 2003

PubMed Abstract: 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 three-dimensional 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.

PubMed: 12606717
DOI: 10.1073/pnas.0538077100

Experimental method

X-RAY DIFFRACTION (2.8 Å)