1zk6
From Proteopedia
(New page: 200px<br /><applet load="1zk6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zk6" /> '''NMR solution structure of B. subtilis PrsA P...) |
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- | [[Image:1zk6.gif|left|200px]]<br /><applet load="1zk6" size=" | + | [[Image:1zk6.gif|left|200px]]<br /><applet load="1zk6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zk6" /> | caption="1zk6" /> | ||
'''NMR solution structure of B. subtilis PrsA PPIase'''<br /> | '''NMR solution structure of B. subtilis PrsA PPIase'''<br /> | ||
==Overview== | ==Overview== | ||
- | PrsA is a peptidyl-prolyl isomerase (PPIase) from Bacillus subtilis | + | PrsA is a peptidyl-prolyl isomerase (PPIase) from Bacillus subtilis belonging to the parvulin family of PPIases. It is a membrane bound lipoprotein at the membrane-wall interface, involved in folding of exported proteins. We present the NMR solution structure of the PPIase domain of PrsA, the first from a Gram-positive bacterium. In addition we mapped out the active site with NMR titration experiments. A high degree of conservation with other members of the parvulin family was revealed in the structure and binding site. Interactions with substrate peptides were also characterized by mutated domains revealing that H122 is indispensable for overall correct folding. |
==About this Structure== | ==About this Structure== | ||
- | 1ZK6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. 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:// | + | 1ZK6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. 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=1ZK6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Kilpelainen, I.]] | [[Category: Kilpelainen, I.]] | ||
[[Category: Permi, P.]] | [[Category: Permi, P.]] | ||
- | [[Category: Purhonen, S | + | [[Category: Purhonen, S L.]] |
[[Category: Sarvas, M.]] | [[Category: Sarvas, M.]] | ||
[[Category: Seppala, R.]] | [[Category: Seppala, R.]] | ||
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[[Category: alpha/beta structure]] | [[Category: alpha/beta structure]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:21 2008'' |
Revision as of 14:16, 21 February 2008
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NMR solution structure of B. subtilis PrsA PPIase
Overview
PrsA is a peptidyl-prolyl isomerase (PPIase) from Bacillus subtilis belonging to the parvulin family of PPIases. It is a membrane bound lipoprotein at the membrane-wall interface, involved in folding of exported proteins. We present the NMR solution structure of the PPIase domain of PrsA, the first from a Gram-positive bacterium. In addition we mapped out the active site with NMR titration experiments. A high degree of conservation with other members of the parvulin family was revealed in the structure and binding site. Interactions with substrate peptides were also characterized by mutated domains revealing that H122 is indispensable for overall correct folding.
About this Structure
1ZK6 is a Single protein structure of sequence from Bacillus subtilis. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Full crystallographic information is available from OCA.
Reference
NMR solution structure and characterization of substrate binding site of the PPIase domain of PrsA protein from Bacillus subtilis., Tossavainen H, Permi P, Purhonen SL, Sarvas M, Kilpelainen I, Seppala R, FEBS Lett. 2006 Mar 20;580(7):1822-6. Epub 2006 Feb 24. PMID:16516208
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