1m5y: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1m5y.jpg|left|200px]]<br /><applet load="1m5y" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1m5y, resolution 3.00&Aring;" />
caption="1m5y, resolution 3.00&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M5Y OCA].  
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.B.]]
[[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]]


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