2WC8
S100A12 complex with zinc in the absence of calcium
Summary for 2WC8
| Entry DOI | 10.2210/pdb2wc8/pdb |
| Related | 1E8A 1GQM 1ODB 2WCB 2WCE 2WCF |
| Descriptor | PROTEIN S100-A12, SODIUM ION, ZINC ION, ... (5 entities in total) |
| Functional Keywords | calcium signalling, ef-hand, calcium free, s100 protein, host-parasite response, metal binding protein |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 4 |
| Total formula weight | 43718.57 |
| Authors | Moroz, O.V.,Blagova, E.V.,Wilkinson, A.J.,Wilson, K.S.,Bronstein, I.B. (deposition date: 2009-03-10, release date: 2009-06-23, Last modification date: 2023-12-13) |
| Primary citation | Moroz, O.V.,Blagova, E.V.,Wilkinson, A.J.,Wilson, K.S.,Bronstein, I.B. The Crystal Structures of Human S100A12 in Apo Form and in Complex with Zinc: New Insights Into S100A12 Oligomerisation. J.Mol.Biol., 391:536-, 2009 Cited by PubMed Abstract: The functions of the members of the S100 family of EF-hand proteins are modulated by calcium and, in a number of cases, by zinc or copper. One such protein is S100A12, which is implicated in inflammation and host-parasite responses. Previously, we reported the structures of human S100A12 in both low (dimeric) and high (hexameric) calcium forms and, in addition, that of a complex with copper and calcium. Here we report the crystal structures of the metal-free apo form of human S100A12 at 1.77 A resolution and of the zinc complex in two crystal forms (P2(1)2(1)2(1) and F222) to 1.88 A and 1.73 A resolution, respectively. These are the first structures of a zinc-only complex of an S100 protein to be determined. The zinc complex structure shows significant differences from those of both calcium-loaded and apo-S100A12 structures, and comparisons suggest an explanation for the zinc-induced 1500-fold increase in calcium affinity. In addition, the new structures provide insight into the role of zinc-calcium interplay in the transition of S100A12 from a dimer through a tetramer to a hexamer. The role of both zinc and calcium in target binding by S100A12 during host-parasite responses is confirmed by experiments with paramyosin from the tropical parasites Onchocerca volvulus and Brugia malayi. PubMed: 19501594DOI: 10.1016/J.JMB.2009.06.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.88 Å) |
Structure validation
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