2WCF

calcium-free (apo) S100A12

Summary for 2WCF

• Entry DOI: 10.2210/pdb2wcf/pdb
• Related: 1E8A 1GQM 1ODB 2WC8 2WCB 2WCE
• Descriptor: PROTEIN S100-A12, SODIUM ION (3 entities in total)
• Functional Keywords: calcium signalling, apo, ef-hand, calcium free, s100 protein, host-parasite response, metal binding protein
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 6
• Total formula weight: 64805.25

Authors

Moroz, O.V.,Blagova, E.V.,Wilkinson, A.J.,Wilson, K.S.,Bronstein, I.B. (deposition date: 2009-03-11, 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

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: 19501594
DOI: 10.1016/J.JMB.2009.06.004

Experimental method

X-RAY DIFFRACTION (2.78 Å)