1OEK
YodA from Escherichia coli crystallised with zinc ions
Summary for 1OEK
| Entry DOI | 10.2210/pdb1oek/pdb |
| Descriptor | METAL-BINDING PROTEIN ZINT, ZINC ION (3 entities in total) |
| Functional Keywords | metal binding protein, stress protein, lipocalin, yoda |
| Biological source | ESCHERICHIA COLI |
| Cellular location | Cytoplasm : P76344 |
| Total number of polymer chains | 1 |
| Total formula weight | 22635.51 |
| Authors | David, G.,Blondeau, K.,Renouard, M.,Penel, S.,Lewit-Bentley, A. (deposition date: 2003-03-28, release date: 2003-08-15, Last modification date: 2024-11-06) |
| Primary citation | David, G.,Blondeau, K.,Schiltz, M.,Penel, S.,Lewit-Bentley, A. Yoda from Escherichia Coli is a Metal-Binding, Lipocalin-Like Protein J.Biol.Chem., 278:43728-, 2003 Cited by PubMed Abstract: We have determined the crystal structure of YodA, an Escherichia coli protein of unknown function. YodA had been identified under conditions of cadmium stress, and we confirm that it binds metals such as cadmium and zinc. We have also found nickel bound in one of the crystal forms. YodA is composed of two domains: a main lipocalin/calycin-like domain and a helical domain. The principal metal-binding site lies on one side of the calycin domain, thus making YodA the first metal-binding lipocalin known. Our experiments suggest that YodA expression may be part of a more general stress response. From sequence analogy with the C-terminal domain of a metal-binding receptor of a member of bacterial ATP-binding cassette transporters, we propose a three-dimensional model for this receptor and suggest that YodA may have a receptor-type partner in E. coli. PubMed: 12909634DOI: 10.1074/JBC.M304484200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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