2C0G
Structure of PDI-related Chaperone, Wind mutant-Y53S
Summary for 2C0G
| Entry DOI | 10.2210/pdb2c0g/pdb |
| Related | 1OVN 2C0E 2C0F 2C1Y |
| Descriptor | WINDBEUTEL PROTEIN, SODIUM ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | wind, windbeutel, pdi-dbeta, pdi, protein disulfide isomerase, pipe, dorsal-ventral patterning, chaperone, wind mutants, developmental protein, endoplasmic reticulum |
| Biological source | DROSOPHILA MELANOGASTER (FRUIT FLY) |
| Cellular location | Endoplasmic reticulum lumen : O44342 |
| Total number of polymer chains | 2 |
| Total formula weight | 57001.30 |
| Authors | Sevvana, M.,Ma, Q.,Barnewitz, K.,Guo, C.,Soling, H.-D.,Ferrari, D.M.,Sheldrick, G.M. (deposition date: 2005-09-02, release date: 2006-08-29, Last modification date: 2024-11-20) |
| Primary citation | Sevvana, M.,Biadene, M.,Ma, Q.,Guo, C.,Soling, H.-D.,Sheldrick, G.M.,Ferrari, D.M. Structural Elucidation of the Pdi-Related Chaperone Wind with the Help of Mutants. Acta Crystallogr.,Sect.D, 62:589-, 2006 Cited by PubMed Abstract: The structures of the PDI-related protein Wind (with a C-terminal His(6) tag) and the mutants Y53S, Y53F and Y55K have been determined and compared with the wild-type structure with the His(6) tag at the N-terminus. All five structures show the same mode of dimerization, showing that this was not an artefact introduced by the nearby N-terminal His(6) tag and suggesting that this dimer may also be the biologically active form. Although the mutants Y53S and Y55K completely abrogate transport of the protein Pipe (which appears to be the primary function of Wind in the cell), only subtle differences can be seen in the putative Pipe-binding region. The Pipe binding in the active forms appears to involve hydrophobic interactions between aromatic systems, whereas the inactive mutants may be able to bind more strongly with the help of hydrogen bonds, which could disturb the delicate equilibrium required for effective Pipe transport. PubMed: 16699185DOI: 10.1107/S0907444906010456 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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