1WS8
Crystal Structure of Mavicyanin from Cucurbita pepo medullosa (Zucchini)
Summary for 1WS8
| Entry DOI | 10.2210/pdb1ws8/pdb |
| Related | 1WS7 |
| Descriptor | mavicyanin, COPPER (II) ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | mavicyanin, oxidized form, phytocyanin, cupredoxin, electron transport |
| Biological source | Cucurbita pepo |
| Total number of polymer chains | 4 |
| Total formula weight | 48003.34 |
| Authors | Xie, Y.,Inoue, T.,Miyamoto, Y.,Matsumura, H.,Kunishige, K.,Yamaguchi, K.,Nojini, M.,Suzuki, S.,Kai, Y. (deposition date: 2004-11-02, release date: 2004-11-23, Last modification date: 2011-07-13) |
| Primary citation | Xie, Y.,Inoue, T.,Miyamoto, Y.,Matsumura, H.,Kataoka, K.,Yamaguchi, K.,Nojini, M.,Suzuki, S.,Kai, Y. Structural reorganization of the copper binding site involving Thr15 of mavicyanin from Cucurbita pepo medullosa (zucchini) upon reduction. J.Biochem.(Tokyo), 137:455-461, 2005 Cited by PubMed Abstract: Mavicyanin, a glycosylated protein isolated from Cucurbita pepo medullosa (zucchini), is a member of the phytocyanin subfamily containing one polypeptide chain of 109 amino residues and an unusual type-I Cu site in which the copper ligands are His45, Cys86, His91, and Gln96. The crystal structures of oxidized and reduced mavicyanin were determined at 1.6 and 1.9 A resolution, respectively. Mavicyanin has a core structure of seven polypeptide beta-strands arranged as a beta-sandwich organized into two beta-sheets, and the structure considerably resembles that of stellacyanin from cucumber (CST) or cucumber basic protein (CBP). A flexible region was not observed on superimpositioning of the oxidized and reduced mavicyanin structures. However, the Cu(II)-epsilon-O-Gln96 bond length was extended by 0.47 A, and the Thr15 residue was rotated by 60.0 degrees and O-gamma1-Thr15 moved from a distance of 4.78 to 2.58 A from the ligand Gln96 forming a new hydrogen bond between O-gamma1-Thr15 and epsilon-O-Gln96 upon reduction. The reorganization of copper coordination geometry of mavicyanin upon reduction arouses reduction potential decreased above pH 8 [Battistuzzi et al. (2001) J. Inorg. Biochem. 83, 223-227]. The rotation of Thr15 and the hydrogen bonding with the ligand Gln96 may constitute structural evidence of the decrease in the reduction potential at high pH. PubMed: 15858169DOI: 10.1093/jb/mvi062 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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