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1tf2

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(New page: 200px<br /><applet load="1tf2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tf2, resolution 2.90&Aring;" /> '''Crystal structure of...)
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Revision as of 01:05, 21 November 2007

Image:1tf2.jpg

1tf2, resolution 2.90Å

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Crystal structure of SecA:ADP 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

1TF2 is a Single protein structure of sequence from Bacillus subtilis with MG and ADP as ligands. 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

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