2nul

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[[Image:2nul.jpg|left|200px]]<br /><applet load="2nul" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2nul.jpg|left|200px]]
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caption="2nul, resolution 2.1&Aring;" />
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'''PEPTIDYLPROLYL ISOMERASE FROM E. COLI'''<br />
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{{Structure
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|PDB= 2nul |SIZE=350|CAPTION= <scene name='initialview01'>2nul</scene>, resolution 2.1&Aring;
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|SITE=
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|LIGAND=
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|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]
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|GENE=
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}}
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'''PEPTIDYLPROLYL ISOMERASE FROM E. COLI'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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2NUL 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=2NUL OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9268657 9268657]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9268657 9268657]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Peptidylprolyl isomerase]]
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[[Category: rotamase]]
[[Category: rotamase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:11:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:51:23 2008''

Revision as of 15:51, 20 March 2008

Image:2nul.jpg


PDB ID 2nul

Drag the structure with the mouse to rotate
, resolution 2.1Å
Activity: Peptidylprolyl isomerase, with EC number 5.2.1.8
Coordinates: save as pdb, mmCIF, xml



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. 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

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