1nl3

File:1nl3.gif

spinqualitylabelsall models PDB ID 1nl3 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.800Å
Gene:	SECA1 OR SECA OR RV3240C (Mycobacterium tuberculosis)
Domains:	SecA_SW, SecA_PP_bind, DEXDc, PRK12904
Resources:	FirstGlance, OCA, PDBsum, JenaLib, RCSB
Coordinates:	save as pdb, mmCIF, xml

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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