1nkt

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(New page: 200px<br /><applet load="1nkt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nkt, resolution 2.601&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1nkt.gif|left|200px]]<br /><applet load="1nkt" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1nkt, resolution 2.601&Aring;" />
caption="1nkt, resolution 2.601&Aring;" />
'''CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS COMPLEX WITH ADPBS'''<br />
'''CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS COMPLEX WITH ADPBS'''<br />
==Overview==
==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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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 Structure==
==About this Structure==
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1NKT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NKT OCA].
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1NKT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NKT OCA].
==Reference==
==Reference==
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[[Category: Braunstein, M.]]
[[Category: Braunstein, M.]]
[[Category: Holzenburg, A.]]
[[Category: Holzenburg, A.]]
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[[Category: Jr., W.R.Jacobs.]]
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[[Category: Jr., W R.Jacobs.]]
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[[Category: Ronning, D.R.]]
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[[Category: Ronning, D R.]]
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[[Category: Sacchettini, J.C.]]
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[[Category: Sacchettini, J C.]]
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[[Category: Savva, C.G.]]
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[[Category: Savva, C G.]]
[[Category: Sharma, V.]]
[[Category: Sharma, V.]]
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[[Category: TBSGC, TB.Structural.Genomics.Consortium.]]
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[[Category: TBSGC, TB Structural Genomics Consortium.]]
[[Category: ADP]]
[[Category: ADP]]
[[Category: MG]]
[[Category: MG]]
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[[Category: transmembrane transport]]
[[Category: transmembrane transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:20:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:08 2008''

Revision as of 12:07, 21 February 2008


1nkt, resolution 2.601Å

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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.

About this Structure

1NKT is a Single protein structure of sequence from Mycobacterium tuberculosis with and as ligands. 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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