2rqs

3D structure of Pin from the psychrophilic archeon Cenarcheaum symbiosum (CsPin)

spinqualitylabelsall models 2rqs, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2rqs is a 1 chain structure with sequence from Cenarchaeum symbiosum. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: pinA (Cenarchaeum symbiosum) Activity: Peptidylprolyl isomerase, with EC number 5.2.1.8 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Parvulins are a group of peptidyl-prolyl isomerases (PPIases) responsible for important biological processes in all kingdoms of life. The PinA protein from the psychrophilic archaeon Cenarchaeum symbiosum is a parvulin-like PPIase. Due to its striking similarity to the human parvulins Pin1 and Par14, PinA constitutes an interesting subject for structural and functional studies. Here, we present the first high resolution NMR structure of an archaeal parvulin, PinA, based on 1798 conformational restraints. Structure calculation yields an ensemble of 20 convergent low energy structures with a backbone r.m.s.d. value of 0.6 A within the secondary structure elements. The overall fold of PinA comprises the beta-alpha(3)-beta-alpha-beta(2) fold typical for all parvulin structures known so far, but with helix III being a short 3(10)-helix. A detailed comparison of this high resolution structure of the first archaeal PinA protein with bacterial and eukaryotic parvulin PPIase structures reveals an atypically large catalytic binding site. This feature provides an explanation for cold-adapted protein function. Moreover, the residues in and around 3(10)-helix III exhibit strong intramolecular dynamics on a microsecond to millisecond timescale and display structural heterogeneity within the NMR ensemble. A putative peptide ligand was found for PinA by phage display and was used for (1)H-(15)N-HSQC titrations. Again, the flexible region around 3(10)-helix III as well as residues of the peptide binding pocket showed the strongest chemical shift perturbations upon peptide binding. The local flexibility of this region also was modulated by ligand binding. A glycine and two positively charged residues are conserved in most parvulin proteins in this flexible loop region, which may be of general functional importance for parvulin-type PPIases. Structure and Dynamics of the First Archaeal Parvulin Reveal a New Functionally Important Loop in Parvulin-type Prolyl Isomerases.,Jaremko L, Jaremko M, Elfaki I, Mueller JW, Ejchart A, Bayer P, Zhukov I J Biol Chem. 2011 Feb 25;286(8):6554-65. Epub 2010 Dec 7. PMID:21138844 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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