The structure of SecB/OmpA as visualized by electron microscopy: The mature region of the precursor protein binds asymmetrically to SecB.

Abstract:

:SecB, a molecular chaperone in Escherichia coli, binds a subset of precursor proteins that are exported across the plasma membrane via the Sec pathway. Previous studies showed that SecB bound directly to the mature region rather than to the signal sequence of the precursor protein. To determine the binding pattern of SecB and the mature region of the preprotein, here, we visualized the structure of the SecB/OmpA complex by electron microscopy. This complex is composed by two parts: the main density represents one SecB tetramer and the unfolded part of OmpA wrapping round it; the elongated smaller density represents the rest of OmpA. Each SecB protomer makes a different contribution to the binding of SecB with OmpA. The binding pattern between SecB tetramer and OmpA is asymmetric.

authors

Tang Y,Pan X,Tai PC,Sui SF

doi

10.1016/j.bbrc.2010.02.062

subject

Has Abstract

pub_date

2010-03-19 00:00:00

pages

698-702

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(10)00282-2

journal_volume

393

pub_type

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