Summary for 4YD9
| Entry DOI | 10.2210/pdb4yd9/pdb |
| Descriptor | hemocyanin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total) |
| Functional Keywords | decamer, supermolecule, oxygen transport |
| Biological source | Todarodes pacificus More |
| Total number of polymer chains | 30 |
| Total formula weight | 3835835.70 |
| Authors | Matsuno, A.,Gai, Z.,Kato, K.,Tanaka, Y.,Yao, M. (deposition date: 2015-02-21, release date: 2015-10-14, Last modification date: 2023-11-08) |
| Primary citation | Gai, Z.,Matsuno, A.,Kato, K.,Kato, S.,Khan, M.R.I.,Shimizu, T.,Yoshioka, T.,Kato, Y.,Kishimura, H.,Kanno, G.,Miyabe, Y.,Terada, T.,Tanaka, Y.,Yao, M. Crystal Structure of the 3.8-MDa Respiratory Supermolecule Hemocyanin at 3.0 angstrom Resolution Structure, 23:2204-2212, 2015 Cited by PubMed Abstract: Molluscan hemocyanin, a copper-containing oxygen transporter, is one of the largest known proteins. Although molluscan hemocyanins are currently applied as immunotherapeutic agents, their precise structure has not been determined because of their enormous size. Here, we have determined the first X-ray crystal structure of intact molluscan hemocyanin. The structure unveiled the architecture of the 3.8-MDa supermolecule composed of homologous functional units (FUs), wherein the dimers of FUs hierarchically associated to form the entire cylindrical decamer. Most of the specific inter-FU interactions were localized at narrow regions in the FU dimers, suggesting that rigid FU dimers formed by specific interactions assemble with flexibility. Furthermore, the roles of carbohydrates in assembly and allosteric effect, and conserved sulfur-containing residues in copper incorporation, were revealed. The precise structural information obtained in this study will accelerate our understanding of the molecular basis of hemocyanin and its future applications. PubMed: 26602184DOI: 10.1016/j.str.2015.09.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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