6hmz

Crystal Structure of a Single-Domain Cyclophilin from Brassica napus Phloem Sap

spinqualitylabelsall models 6hmz, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6hmz is a 2 chain structure with sequence from Brassica napus and Tolypocladium inflatum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.98Å Ligands: ABA, BMT, DAL, MG, MLE, MLI, MVA, SAR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A078GRH6_BRANA PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU363019] Publication Abstract from PubMed Cyclophilins (CYPs) are a group of ubiquitous prolyl cis/trans isomerases (PPIases). It was shown that plants possess the most diverse CYP families and that these are abundant in the phloem long-distance translocation stream. Since phloem exudate showed PPIase activity, three single-domain CYPs that occur in phloem samples from Brassica napus were characterised on functional and structural levels. It could be shown that they exhibit isomerase activity and that this activity is controlled by a redox regulation mechanism, which has been postulated for divergent CYPs. The structure determination by small-angle X-ray scattering experiments revealed a conserved globular shape. In addition, the high-resolution crystal structure of BnCYP19-1 was resolved and refined to 2.0 A resolution, and the active sites of related CYPs as well as substrate binding were modelled. The obtained data and results support the hypothesis that single domain phloem CYPs are active phloem PPIases that may function as chaperones. Enzyme activity and structural features of three single-domain phloem cyclophilins from Brassica napus.,Hanhart P, Falke S, Garbe M, Rose V, Thiess M, Betzel C, Kehr J Sci Rep. 2019 Jun 27;9(1):9368. doi: 10.1038/s41598-019-45856-y. PMID:31249367 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Peptidyl-prolyl cis-trans isomerase 3D structures

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