1w74

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[[Image:1w74.gif|left|200px]]
[[Image:1w74.gif|left|200px]]
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{{Structure
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|PDB= 1w74 |SIZE=350|CAPTION= <scene name='initialview01'>1w74</scene>, resolution 2.60&Aring;
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The line below this paragraph, containing "STRUCTURE_1w74", creates the "Structure Box" on the page.
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|SITE=
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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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{{STRUCTURE_1w74| PDB=1w74 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w74 OCA], [http://www.ebi.ac.uk/pdbsum/1w74 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w74 RCSB]</span>
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'''X-RAY STRUCTURE OF PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A, PPIA, RV0009, FROM MYCOBACTERIUM TUBERCULOSIS.'''
'''X-RAY STRUCTURE OF PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A, PPIA, RV0009, FROM MYCOBACTERIUM TUBERCULOSIS.'''
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[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: Unge, T.]]
[[Category: Unge, T.]]
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[[Category: cyclophilin]]
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[[Category: Cyclophilin]]
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[[Category: peptidyl-prolyl cis-trans isomerase]]
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[[Category: Peptidyl-prolyl cis-trans isomerase]]
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[[Category: ppiase]]
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[[Category: Ppiase]]
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[[Category: rotamase]]
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[[Category: Rotamase]]
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[[Category: rv0009]]
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[[Category: Rv0009]]
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[[Category: spine]]
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[[Category: Spine]]
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[[Category: structural genomic]]
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[[Category: Structural genomic]]
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[[Category: structural proteomics in europe]]
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[[Category: Structural proteomics in europe]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:13:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:32:05 2008''
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Revision as of 05:13, 13 April 2008

Image:1w74.gif

Template:STRUCTURE 1w74

X-RAY STRUCTURE OF PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A, PPIA, RV0009, FROM MYCOBACTERIUM TUBERCULOSIS.


Overview

Peptidyl-prolyl cis-trans isomerases (EC 5.2.1.8) catalyse the interconversion of cis and trans peptide bonds and are therefore considered to be important for protein folding. They are also thought to participate in processes such as signalling, cell surface recognition, chaperoning and heat-shock response. Here we report the soluble expression of recombinant Mycobacterium tuberculosis peptidyl-prolyl cis-trans isomerase PpiA in Escherichia coli, together with an investigation of its structure and biochemical properties. The protein was shown to be active in a spectrophotometric assay, with an estimated kcat/Km of 2.0 x 10(6) m(-1).s(-1). The X-ray structure of PpiA was solved by molecular replacement, and refined to a resolution of 2.6 A with R and Rfree values of 21.3% and 22.9%, respectively. Comparisons to known structures show that the PpiA represents a slight variation on the peptidyl-prolyl cis-trans isomerase fold, previously not represented in the Protein Data Bank. Inspection of the active site suggests that specificity for substrates and cyclosporin A will be similar to that found for most other enzymes of this structural family. Comparison to the sequence of the second M. tuberculosis enzyme, PpiB, suggests that binding of peptide substrates as well as cyclosporin A may differ in that case.

About this Structure

1W74 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

X-ray structure of peptidyl-prolyl cis-trans isomerase A from Mycobacterium tuberculosis., Henriksson LM, Johansson P, Unge T, Mowbray SL, Eur J Biochem. 2004 Oct;271(20):4107-13. PMID:15479239 Page seeded by OCA on Sun Apr 13 08:13:37 2008

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