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-[[Image:1nkt.gif|left|200px]]
+{{Seed}}
+[[Image:1nkt.png|left|200px]]
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 {{STRUCTURE_1nkt|  PDB=1nkt  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS COMPLEX WITH ADPBS'''
+===CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS COMPLEX WITH ADPBS===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12606717}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12606717 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12606717}}
 ==About this Structure==
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 [[Category: Tbsgc]]
 [[Category: Transmembrane transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:39:04 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:41:51 2008''