1tf5

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(New page: 200px<br /><applet load="1tf5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tf5, resolution 2.18&Aring;" /> '''Crystal structure of...)
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[[Image:1tf5.jpg|left|200px]]<br /><applet load="1tf5" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1tf5.jpg|left|200px]]<br /><applet load="1tf5" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1tf5, resolution 2.18&Aring;" />
caption="1tf5, resolution 2.18&Aring;" />
'''Crystal structure of SecA in an open conformation from Bacillus Subtilis'''<br />
'''Crystal structure of SecA in an open conformation from Bacillus Subtilis'''<br />
==Overview==
==Overview==
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The ATPase SecA mediates the posttranslational translocation of a wide, range of polypeptide substrates through the SecY channel in the, cytoplasmic membrane of bacteria. We have determined the crystal structure, of a monomeric form of Bacillus subtilis SecA at a 2.2-A resolution. A, comparison with the previously determined structures of SecA reveals a, nucleotide-independent, large conformational change that opens a deep, groove similar to that in other proteins that interact with diverse, polypeptides. We propose that the open form of SecA represents an, activated state.
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The ATPase SecA mediates the posttranslational translocation of a wide range of polypeptide substrates through the SecY channel in the cytoplasmic membrane of bacteria. We have determined the crystal structure of a monomeric form of Bacillus subtilis SecA at a 2.2-A resolution. A comparison with the previously determined structures of SecA reveals a nucleotide-independent, large conformational change that opens a deep groove similar to that in other proteins that interact with diverse polypeptides. We propose that the open form of SecA represents an activated state.
==About this Structure==
==About this Structure==
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1TF5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TF5 OCA].
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1TF5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TF5 OCA].
==Reference==
==Reference==
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Jr., W.M.Clemons.]]
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[[Category: Jr., W M.Clemons.]]
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[[Category: Osborne, A.R.]]
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[[Category: Osborne, A R.]]
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[[Category: Rapoport, T.A.]]
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[[Category: Rapoport, T A.]]
[[Category: atpase]]
[[Category: atpase]]
[[Category: helicase]]
[[Category: helicase]]
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[[Category: translocation]]
[[Category: translocation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:12:52 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:56 2008''

Revision as of 13:12, 21 February 2008


1tf5, resolution 2.18Å

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Crystal structure of SecA in an open conformation from Bacillus Subtilis

Overview

The ATPase SecA mediates the posttranslational translocation of a wide range of polypeptide substrates through the SecY channel in the cytoplasmic membrane of bacteria. We have determined the crystal structure of a monomeric form of Bacillus subtilis SecA at a 2.2-A resolution. A comparison with the previously determined structures of SecA reveals a nucleotide-independent, large conformational change that opens a deep groove similar to that in other proteins that interact with diverse polypeptides. We propose that the open form of SecA represents an activated state.

About this Structure

1TF5 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

A large conformational change of the translocation ATPase SecA., Osborne AR, Clemons WM Jr, Rapoport TA, Proc Natl Acad Sci U S A. 2004 Jul 27;101(30):10937-42. Epub 2004 Jul 15. PMID:15256599

Page seeded by OCA on Thu Feb 21 15:12:56 2008

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