1w74
From Proteopedia
(New page: 200px<br /><applet load="1w74" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w74, resolution 2.60Å" /> '''X-RAY STRUCTURE OF P...) |
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| - | [[Image:1w74.gif|left|200px]]<br /><applet load="1w74" size=" | + | [[Image:1w74.gif|left|200px]]<br /><applet load="1w74" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1w74, resolution 2.60Å" /> | caption="1w74, resolution 2.60Å" /> | ||
'''X-RAY STRUCTURE OF PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A, PPIA, RV0009, FROM MYCOBACTERIUM TUBERCULOSIS.'''<br /> | '''X-RAY STRUCTURE OF PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A, PPIA, RV0009, FROM MYCOBACTERIUM TUBERCULOSIS.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Peptidyl-prolyl cis-trans isomerases (EC 5.2.1.8) catalyse the | + | 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== | ==About this Structure== | ||
| - | 1W74 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. 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:// | + | 1W74 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. 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=1W74 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Henriksson, L | + | [[Category: Henriksson, L M.]] |
[[Category: Johansson, P.]] | [[Category: Johansson, P.]] | ||
| - | [[Category: Mowbray, S | + | [[Category: Mowbray, S L.]] |
| - | [[Category: SPINE, Structural | + | [[Category: SPINE, Structural Proteomics in Europe.]] |
[[Category: Unge, T.]] | [[Category: Unge, T.]] | ||
[[Category: cyclophilin]] | [[Category: cyclophilin]] | ||
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[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:09 2008'' |
Revision as of 13:41, 21 February 2008
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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. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 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 Thu Feb 21 15:41:09 2008
Categories: Mycobacterium tuberculosis | Peptidylprolyl isomerase | Single protein | Henriksson, L M. | Johansson, P. | Mowbray, S L. | SPINE, Structural Proteomics in Europe. | Unge, T. | Cyclophilin | Peptidyl-prolyl cis-trans isomerase | Ppiase | Rotamase | Rv0009 | Spine | Structural genomics | Structural proteomics in europe
