1nl3

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{{STRUCTURE_1nl3| PDB=1nl3 | SCENE= }}
{{STRUCTURE_1nl3| PDB=1nl3 | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS in APO FORM'''
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===CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS in APO FORM===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12606717 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12606717}}
==About this Structure==
==About this Structure==
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[[Category: Tbsgc]]
[[Category: Tbsgc]]
[[Category: Transmembrane transport]]
[[Category: Transmembrane transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:39:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:39:28 2008''

Revision as of 11:39, 27 July 2008

Image:1nl3.png

Template:STRUCTURE 1nl3

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

Template:ABSTRACT PUBMED 12606717

About this Structure

1NL3 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

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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