1nl3
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CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS in APO FORM
OverviewOverview
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.
About this StructureAbout this Structure
1NL3 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase., Sharma V, Arockiasamy A, Ronning DR, Savva CG, Holzenburg A, Braunstein M, Jacobs WR Jr, Sacchettini JC, Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2243-8. Epub 2003 Feb 26. PMID:12606717
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- Mycobacterium tuberculosis
- Single protein
- Arockiasamy, A.
- Braunstein, M.
- Holzenburg, A.
- Jr., W.R.Jacobs.
- Ronning, D.R.
- Sacchettini, J.C.
- Savva, C.G.
- Sharma, V.
- TBSGC, TB.Structural.Genomics.Consortium.
- Atpase
- Helicase-like motor domain
- Preprotein translocation
- Protein structure initiative
- Psi
- Structural genomics
- Tb structural genomics consortium
- Tbsgc
- Transmembrane transport