2nul

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[[Image:2nul.jpg|left|200px]]
[[Image:2nul.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2nul |SIZE=350|CAPTION= <scene name='initialview01'>2nul</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_2nul", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_2nul| PDB=2nul | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nul OCA], [http://www.ebi.ac.uk/pdbsum/2nul PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nul RCSB]</span>
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}}
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'''PEPTIDYLPROLYL ISOMERASE FROM E. COLI'''
'''PEPTIDYLPROLYL ISOMERASE FROM E. COLI'''
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[[Category: Edwards, K J.]]
[[Category: Edwards, K J.]]
[[Category: Ollis, D L.]]
[[Category: Ollis, D L.]]
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[[Category: isomerase]]
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[[Category: Isomerase]]
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[[Category: rotamase]]
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[[Category: Rotamase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:55:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:08:39 2008''
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Revision as of 06:55, 4 May 2008

Image:2nul.jpg

Template:STRUCTURE 2nul

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 Page seeded by OCA on Sun May 4 09:55:50 2008

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