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1m5y
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(New page: 200px<br /><applet load="1m5y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m5y, resolution 3.00Å" /> '''Crystallographic Str...)
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Revision as of 19:03, 20 November 2007
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Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding
Overview
The SurA protein facilitates correct folding of outer membrane proteins in, gram-negative bacteria. The sequence of Escherichia coli SurA presents, four segments, two of which are peptidyl-prolyl isomerases (PPIases); the, crystal structure reveals an asymmetric dumbbell, in which the, amino-terminal, carboxy-terminal, and first PPIase segments of the, sequence form a core structural module, and the second PPIase segment is a, satellite domain tethered approximately 30 A from this module. The core, module, which is implicated in membrane protein folding, has a novel fold, that includes an extended crevice. Crystal contacts show that peptides, bind within the crevice, suggesting a model for chaperone activity whereby, segments of polypeptide may be repetitively sequestered and released, during the membrane protein-folding process.
About this Structure
1M5Y is a Single protein structure of sequence from Escherichia coli. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Full crystallographic information is available from OCA.
Reference
Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins., Bitto E, McKay DB, Structure. 2002 Nov;10(11):1489-98. PMID:12429090
Page seeded by OCA on Tue Nov 20 21:10:17 2007
