4yn3

Crystal structure of Cucumisin complex with pro-peptide

spinqualitylabelsall models 4yn3, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4yn3 is a 2 chain structure with sequence from Cucumis melo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, CL, FUC, GOL, MAN, NAG, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CUCM1_CUCME Publication Abstract from PubMed Cucumisin [EC 3.4.21.25], a subtilisin-like serine endopeptidase, was isolated from melon fruit, Cucumis melo L. Mature cucumisin (67 kDa, 621 residues) is produced by removal of the propeptide (10 kDa, 88 residues) from the cucumisin precursor by subsequence processing. It is reported that cucumisin is inhibited by its own propeptide. The crystal structure of mature cucumisin is reported to be composed of three domains: the subtilisin-like catalytic domain, the protease-associated domain and the C-terminal fibronectin-III-like domain. In this study, the crystal structure of the mature cucumisin*propeptide complex was determined by the molecular replacement method and refined at 1.95 A resolution. In this complex, the propeptide had a domain of the alpha-beta sandwich motif with four-stranded antiparallel beta-sheets, two helices and a strand of the C-terminal region. The beta-sheets of the propeptide bind to two parallel surface helices of cucumisin through hydrophobic interaction and 27 hydrogen bonds. The C-terminus of the propeptide binds to the cleft of the active site as peptide substrates. The inhibitory assay suggested that the C-terminal seven residues of the propeptide do not inhibit the cucumisin activity. The crystal structure of the cucumisin*propeptide complex revealed the regulation mechanism of cucumisin activity. Structural basis of cucumisin protease activity regulation by its propeptide.,Sotokawauchi A, Kato-Murayama M, Murayama K, Hosaka T, Maeda I, Onjo M, Ohsawa N, Kato DI, Arima K, Shirouzu M J Biochem. 2017 Jan;161(1):45-53. doi: 10.1093/jb/mvw053. Epub 2016 Sep 10. PMID:27616715 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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