3ima | pdb_00003ima

Complex structure of tarocystatin and papain

spinqualitylabelsall models 3ima, resolution 2.03Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ima is a 4 chain structure with sequence from Arum esculentum and Carica papaya. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT NonStd Res: OCS Gene: CPI (Arum esculentum) Activity: Papain, with EC number 3.4.22.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Tarocystatin (CeCPI) from taro (Colocasia esculenta cv. Kaohsiung no. 1), a group-2 phytocystatin, shares a conserved N-terminal cystatin domain (NtD) with other phytocystatins but contains a C-terminal cystatin-like extension (CtE). The structure of the tarocystatin-papain complex and the domain interaction between NtD and CtE in tarocystatin have not been determined. We resolved the crystal structure of the phytocystatin-papain complex at resolution 2.03 A. Surprisingly, the structure of the NtD-papain complex in a stoichiometry of 1:1 could be built, with no CtE observed. Only two remnant residues of CtE could be built in the structure of the CtE-papain complex. Therefore, CtE is easily digested by papain. To further characterize the interaction between NtD and CtE, three segments of tarocystatin, including the full-length (FL), NtD and CtE, were used to analyze the domain-domain interaction and the inhibition ability. The results from glutaraldehyde cross-linking and yeast two-hybrid assay indicated the existence of an intrinsic flexibility in the region linking NtD and CtE for most tarocystatin molecules. In the inhibition activity assay, the glutathione-S-transferase (GST)-fused FL showed the highest inhibition ability without residual peptidase activity, and GST-NtD and FL showed almost the same inhibition ability, which was higher than with NtD alone. On the basis of the structures, the linker flexibility and inhibition activity of tarocystatins, we propose that the overhangs from the cystatin domain may enhance the inhibition ability of the cystatin domain against papain. Crystal structure of tarocystatin-papain complex: implications for the inhibition property of group-2 phytocystatins.,Chu MH, Liu KL, Wu HY, Yeh KW, Cheng YS Planta. 2011 Aug;234(2):243-54. Epub 2011 Mar 18. PMID:21416241 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Papain

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