2nul
From Proteopedia
(New page: 200px<br /><applet load="2nul" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nul, resolution 2.1Å" /> '''PEPTIDYLPROLYL ISOMER...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2nul.jpg|left|200px]]<br /><applet load="2nul" size=" | + | [[Image:2nul.jpg|left|200px]]<br /><applet load="2nul" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2nul, resolution 2.1Å" /> | caption="2nul, resolution 2.1Å" /> | ||
'''PEPTIDYLPROLYL ISOMERASE FROM E. COLI'''<br /> | '''PEPTIDYLPROLYL ISOMERASE FROM E. COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the unliganded form of the Escherichia coli cytoplasmic | + | The structure of the unliganded form of the Escherichia coli cytoplasmic peptidyl-prolyl isomerase (ppiB gene product) in a new crystal form was determined by the molecular replacement method and refined to an R-factor of 16.1% at 2.1 A resolution. The enzyme crystallized in the orthorhombic C2221 space group with unit cell dimensions of a=44.7 A, b=68.2 A and c=102.0 A. Comparison with the reported structure of the enzyme complexed with the tripeptide substrate succinyl-Ala-Pro-Ala-p-nitroanilide revealed subtle changes that occur upon complex formation. There is evidence to suggest that two surface loops have significantly reduced mobility in the complexed structure. |
==About this Structure== | ==About this Structure== | ||
| - | 2NUL 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:// | + | 2NUL 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=2NUL OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Edwards, K | + | [[Category: Edwards, K J.]] |
| - | [[Category: Ollis, D | + | [[Category: Ollis, D L.]] |
[[Category: isomerase]] | [[Category: isomerase]] | ||
[[Category: rotamase]] | [[Category: rotamase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:11:13 2008'' |
Revision as of 16:11, 21 February 2008
|
PEPTIDYLPROLYL ISOMERASE FROM E. COLI
Overview
The structure of the unliganded form of the Escherichia coli cytoplasmic peptidyl-prolyl isomerase (ppiB gene product) in a new crystal form was determined by the molecular replacement method and refined to an R-factor of 16.1% at 2.1 A resolution. The enzyme crystallized in the orthorhombic C2221 space group with unit cell dimensions of a=44.7 A, b=68.2 A and c=102.0 A. Comparison with the reported structure of the enzyme complexed with the tripeptide substrate succinyl-Ala-Pro-Ala-p-nitroanilide revealed subtle changes that occur upon complex formation. There is evidence to suggest that two surface loops have significantly reduced mobility in the complexed structure.
About this Structure
2NUL 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
Crystal structure of cytoplasmic Escherichia coli peptidyl-prolyl isomerase: evidence for decreased mobility of loops upon complexation., Edwards KJ, Ollis DL, Dixon NE, J Mol Biol. 1997 Aug 15;271(2):258-65. PMID:9268657
Page seeded by OCA on Thu Feb 21 18:11:13 2008
