1nl3: Difference between revisions
New page: left|200px<br /><applet load="1nl3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nl3, resolution 2.800Å" /> '''CRYSTAL STRUCTURE O... |
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[[Image:1nl3.gif|left|200px]]<br /><applet load="1nl3" size=" | [[Image:1nl3.gif|left|200px]]<br /><applet load="1nl3" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1nl3, resolution 2.800Å" /> | caption="1nl3, resolution 2.800Å" /> | ||
'''CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS in APO FORM'''<br /> | '''CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS in APO FORM'''<br /> | ||
==Overview== | ==Overview== | ||
In bacteria, the majority of exported proteins are translocated by the Sec | 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== | ||
1NL3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http:// | 1NL3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NL3 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Braunstein, M.]] | [[Category: Braunstein, M.]] | ||
[[Category: Holzenburg, A.]] | [[Category: Holzenburg, A.]] | ||
[[Category: Jr., W | [[Category: Jr., W R.Jacobs.]] | ||
[[Category: Ronning, D | [[Category: Ronning, D R.]] | ||
[[Category: Sacchettini, J | [[Category: Sacchettini, J C.]] | ||
[[Category: Savva, C | [[Category: Savva, C G.]] | ||
[[Category: Sharma, V.]] | [[Category: Sharma, V.]] | ||
[[Category: TBSGC, TB | [[Category: TBSGC, TB Structural Genomics Consortium.]] | ||
[[Category: atpase]] | [[Category: atpase]] | ||
[[Category: helicase-like motor domain]] | [[Category: helicase-like motor domain]] | ||
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[[Category: transmembrane transport]] | [[Category: transmembrane transport]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:16 2008'' | ||
Revision as of 15:07, 21 February 2008
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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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- 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