2nul: Difference between revisions

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[[Image:2nul.jpg|left|200px]]<br /><applet load="2nul" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2nul.jpg|left|200px]]<br /><applet load="2nul" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2nul, resolution 2.1Å" />

'''PEPTIDYLPROLYL ISOMERASE FROM E. COLI'''<br />

==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.

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 [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=2NUL OCA].

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==

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[[Category: Peptidylprolyl isomerase]]

[[Category: Single protein]]

[[Category: Edwards, K.J.]]

[[Category: Edwards, K J.]]

[[Category: Ollis, D.L.]]

[[Category: Ollis, D L.]]

[[Category: isomerase]]

[[Category: rotamase]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 12:55:~~19 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:11:13 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2nul.jpg|left|200px]]<br /><applet load="2nul" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2nul.jpg|left|200px]]<br /><applet load="2nul" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2nul, resolution 2.1&Aring;" />
 '''PEPTIDYLPROLYL ISOMERASE FROM E. COLI'''<br />
 ==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.
+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==
-NUL 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=2NUL OCA].
+NUL 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==
@@ Line 14: / Line 14: @@
 [[Category: Peptidylprolyl isomerase]]
 [[Category: Single protein]]
-[[Category: Edwards, K.J.]]
+[[Category: Edwards, K J.]]
-[[Category: Ollis, D.L.]]
+[[Category: Ollis, D L.]]
 [[Category: isomerase]]
 [[Category: rotamase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:55:19 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:11:13 2008''