1m5y
From Proteopedia
(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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| - | [[Image:1m5y.jpg|left|200px]]<br /><applet load="1m5y" size=" | + | [[Image:1m5y.jpg|left|200px]]<br /><applet load="1m5y" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1m5y, resolution 3.00Å" /> | caption="1m5y, resolution 3.00Å" /> | ||
'''Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding'''<br /> | '''Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The SurA protein facilitates correct folding of outer membrane proteins in | + | 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== | ==About this Structure== | ||
| - | 1M5Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http:// | + | 1M5Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M5Y OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bitto, E.]] | [[Category: Bitto, E.]] | ||
| - | [[Category: McKay, D | + | [[Category: McKay, D B.]] |
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
[[Category: gram negative bacteria]] | [[Category: gram negative bacteria]] | ||
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[[Category: survival protein a]] | [[Category: survival protein a]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:50 2008'' |
Revision as of 11:51, 21 February 2008
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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 Thu Feb 21 13:51:50 2008
