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[[Image: | ==CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS in APO FORM== | ||
<StructureSection load='1nl3' size='340' side='right' caption='[[1nl3]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1nl3]] is a 2 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NL3 FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nkt|1nkt]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SECA1 OR SECA OR RV3240C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nl3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nl3 RCSB], [http://www.ebi.ac.uk/pdbsum/1nl3 PDBsum], [http://www.topsan.org/Proteins/TBSGC/1nl3 TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/SECA1_MYCTU SECA1_MYCTU]] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of precursor proteins, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane (By similarity). | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nl/1nl3_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:12606717</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Preprotein translocase|Preprotein translocase]] | |||
*[[SecA|SecA]] | *[[SecA|SecA]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Arockiasamy, A | [[Category: Arockiasamy, A]] | ||
[[Category: Braunstein, M | [[Category: Braunstein, M]] | ||
[[Category: Holzenburg, A | [[Category: Holzenburg, A]] | ||
[[Category: Jacobs, W R | [[Category: Jacobs, W R]] | ||
[[Category: Ronning, D R | [[Category: Ronning, D R]] | ||
[[Category: Sacchettini, J C | [[Category: Sacchettini, J C]] | ||
[[Category: Savva, C G | [[Category: Savva, C G]] | ||
[[Category: Sharma, V | [[Category: Sharma, V]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Atpase]] | [[Category: Atpase]] | ||
[[Category: Helicase-like motor domain]] | [[Category: Helicase-like motor domain]] | ||
[[Category: Preprotein translocation]] | [[Category: Preprotein translocation]] | ||
[[Category: Protein structure initiative]] | [[Category: PSI, Protein structure initiative]] | ||
[[Category: Protein transport]] | [[Category: Protein transport]] | ||
[[Category: Tbsgc]] | [[Category: Tbsgc]] | ||
[[Category: Transmembrane transport]] | [[Category: Transmembrane transport]] | ||
Revision as of 16:30, 24 December 2014
CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS in APO FORMCRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS in APO FORM
Structural highlights
Function[SECA1_MYCTU] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of precursor proteins, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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