We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2mnt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
 +
==Solution structure of the PPIase domain of TbPar42==
==Solution structure of the PPIase domain of TbPar42==
<StructureSection load='2mnt' size='340' side='right' caption='[[2mnt]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='2mnt' size='340' side='right' caption='[[2mnt]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2mnt]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MNT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MNT FirstGlance]. <br>
<table><tr><td colspan='2'>[[2mnt]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MNT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MNT FirstGlance]. <br>
-
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mnt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mnt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mnt RCSB], [http://www.ebi.ac.uk/pdbsum/2mnt PDBsum]</span></td></tr>
+
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mnt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mnt OCA], [http://pdbe.org/2mnt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mnt RCSB], [http://www.ebi.ac.uk/pdbsum/2mnt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mnt ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
-
Parvulins belong to a family of peptidyl-prolyl cis/trans isomerases (PPIases) that catalyze the cis/trans conformations of prolyl-peptidyl bonds. Herein, we characterized two novel parvulins, TbPIN1 and TbPAR42, in Trypanosoma brucei. TbPIN1, a 115 amino-acid protein, contains a single PPIase domain but lacks the N-terminal WW domain. Using NMR spectroscopy, TbPIN1 was found to exhibit PPIase activity toward a phosphorylated substrate. Overexpression of TbPIN1 can rescue the impaired temperature-sensitive phenotype in a mutant yeast strain. TbPAR42, containing 383 amino acids, comprises a novel FHA domain at its N terminus and a C-terminal PPIase domain but is a non-Pin1-type PPIase. Functionally, a knockdown of TbPAR42 in its procyclic form results in reduced proliferation rates suggesting an important role in cell growth.
+
The parvulin family of peptidyl-prolyl cis/trans isomerases (PPIases) catalyzes the cis/trans isomerization of the peptide bonds preceding Pro residues. Eukaryotic parvulin-type PPIases have been shown to be involved in cell proliferation and cell cycle progression. Here we present the biochemical and molecular characterization of a novel multi-domain parvulin-type PPIase from the human pathogenic Trypanosoma cruzi, annotated as TcPar45. Like most other parvulins, Par45 has an N-terminal extension, but, in contrast to human Pin1, it contains a forkhead-associated domain (FHA) instead of a WW domain at the N-terminal end. Par45 shows a strong preference for a substrate with the basic Arg residue preceding Pro (Suc-Ala-Arg-Pro-Phe-NH-Np: k(cat)/K(M)=97.1 /M/s), like that found for human Par14. In contrast to human Pin1, but similarly to Par14, Par45 does not accelerate the cis/trans interconversion of acidic substrates containing Glu-Pro bonds. It is preferentially located in the parasite nucleus. Single RNA interference (RNAi)-mediated knock-down showed that there was a growth inhibition in procyclic Trypanosoma brucei cells. These results identify Par45 as a phosphorylation-independent parvulin required for normal cell proliferation in a unicellular eukaryotic cell.
-
Functional characterization of two novel parvulins in Trypanosoma brucei.,Goh JY, Lai CY, Tan LC, Yang D, He CY, Liou YC FEBS Lett. 2010 Jul 2;584(13):2901-8. doi: 10.1016/j.febslet.2010.04.077. Epub, 2010 May 11. PMID:20466001<ref>PMID:20466001</ref>
+
Identification of an atypical peptidyl-prolyl cis/trans isomerase from trypanosomatids.,Erben ED, Valguarnera E, Nardelli S, Chung J, Daum S, Potenza M, Schenkman S, Tellez-Inon MT Biochim Biophys Acta. 2010 Sep;1803(9):1028-37. doi:, 10.1016/j.bbamcr.2010.05.006. Epub 2010 May 24. PMID:20580912<ref>PMID:20580912</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
 +
<div class="pdbe-citations 2mnt" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Revision as of 17:31, 18 January 2017

Solution structure of the PPIase domain of TbPar42

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2mnt"
Personal tools