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2mnt

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Current revision (07:05, 2 December 2020) (edit) (undo)
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#REDIRECT [[2n87]] This PDB entry is obsolete and replaced by 2n87
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==Solution structure of the PPIase domain of TbPar42==
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<StructureSection load='2mnt' size='340' side='right'caption='[[2mnt]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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== Structural highlights ==
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<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://proteopedia.org/fgij/fg.htm?mol=2MNT FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2mnt" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Bayer, P]]
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[[Category: Rehic, E]]
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[[Category: Isomerase]]
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[[Category: Ppiase domain]]
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[[Category: Tbpar42]]
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[[Category: Tbpar45]]
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[[Category: Trypanosoma]]
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Current revision

  1. REDIRECT 2n87 This PDB entry is obsolete and replaced by 2n87

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