1m5y
From Proteopedia
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| - | [[Image:1m5y.jpg|left|200px]] | + | [[Image:1m5y.jpg|left|200px]] |
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| - | '''Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding''' | + | {{Structure |
| + | |PDB= 1m5y |SIZE=350|CAPTION= <scene name='initialview01'>1m5y</scene>, resolution 3.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] | ||
| + | |GENE= sura ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1M5Y is a [ | + | 1M5Y is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M5Y OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12429090 12429090] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
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[[Category: membrane protein folding]] | [[Category: membrane protein folding]] | ||
[[Category: periplasmic molecular chaperone]] | [[Category: periplasmic molecular chaperone]] | ||
| - | [[Category: survival protein | + | [[Category: survival protein some]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:39:20 2008'' |
Revision as of 10:39, 20 March 2008
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| , resolution 3.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | sura (Escherichia coli) | ||||||
| Activity: | Peptidylprolyl isomerase, with EC number 5.2.1.8 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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