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1m5y

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{{STRUCTURE_1m5y| PDB=1m5y | SCENE= }}
{{STRUCTURE_1m5y| PDB=1m5y | SCENE= }}
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'''Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding'''
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===Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12429090 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12429090}}
==About this Structure==
==About this Structure==
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[[Category: Periplasmic molecular chaperone]]
[[Category: Periplasmic molecular chaperone]]
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Revision as of 20:17, 2 July 2008

Image:1m5y.png

Template:STRUCTURE 1m5y

Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding

Template:ABSTRACT PUBMED 12429090

About this Structure

1M5Y is a Single protein structure of sequence from Escherichia coli. 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 Wed Jul 2 23:17:10 2008

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