1m5y: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1m5y.jpg|left|200px]] | [[Image:1m5y.jpg|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1m5y", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_1m5y| PDB=1m5y | SCENE= }} | |||
}} | |||
'''Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding''' | '''Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding''' | ||
| Line 28: | Line 25: | ||
[[Category: Bitto, E.]] | [[Category: Bitto, E.]] | ||
[[Category: McKay, D B.]] | [[Category: McKay, D B.]] | ||
[[Category: | [[Category: Crystal structure]] | ||
[[Category: | [[Category: Gram negative bacteria]] | ||
[[Category: | [[Category: Membrane protein folding]] | ||
[[Category: | [[Category: Periplasmic molecular chaperone]] | ||
[[Category: | [[Category: Survival protein some]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:40:34 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 21:40, 2 May 2008
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. 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 Sat May 3 00:40:34 2008
