TY - JOUR
T1 - The Crystal Structure of Zebrafish S100Z
T2 - Implications for Calcium-Promoted S100 Protein Oligomerisation
AU - Moroz, Olga V.
AU - Bronstein, Igor B.
AU - Wilson, Keith S.
PY - 2011/9/2
Y1 - 2011/9/2
N2 - The S100 family, with about 20 members in humans, is composed of EF-hand calcium-regulated proteins and is linked to a range of serious human diseases, including cancer and autoimmune and neurological disorders. The oldest S100 family members are found in teleosts (bony fish). The zebrafish, Danio rerio, was suggested as a promising model system for in vivo studies on S100 family functions, and we chose to investigate zebrafish S100Z as the closest homologue of the metastasis-promoting human S100A4. Here, we report the first crystal structure of an S100 protein from this organism, the calcium-bound state of S100Z to 2.03 angstrom resolution. Crystal packing suggests higher-order oligomerisation of S100Z dimers, with a tetramerisation interface very similar to, but even more extensive than, that reported for S100A4. The interactions are primarily through the C-terminal alpha IV helices from adjacent dimers in an antiparallel orientation. Structural comparisons between known S100 multimeric assemblies together with analysis of calcium-driven changes to the dimerisation cores suggest a mechanism for calcium-promoted oligomerisation of S100 proteins. (C) 2011 Elsevier Ltd. All rights reserved.
AB - The S100 family, with about 20 members in humans, is composed of EF-hand calcium-regulated proteins and is linked to a range of serious human diseases, including cancer and autoimmune and neurological disorders. The oldest S100 family members are found in teleosts (bony fish). The zebrafish, Danio rerio, was suggested as a promising model system for in vivo studies on S100 family functions, and we chose to investigate zebrafish S100Z as the closest homologue of the metastasis-promoting human S100A4. Here, we report the first crystal structure of an S100 protein from this organism, the calcium-bound state of S100Z to 2.03 angstrom resolution. Crystal packing suggests higher-order oligomerisation of S100Z dimers, with a tetramerisation interface very similar to, but even more extensive than, that reported for S100A4. The interactions are primarily through the C-terminal alpha IV helices from adjacent dimers in an antiparallel orientation. Structural comparisons between known S100 multimeric assemblies together with analysis of calcium-driven changes to the dimerisation cores suggest a mechanism for calcium-promoted oligomerisation of S100 proteins. (C) 2011 Elsevier Ltd. All rights reserved.
UR - http://www.scopus.com/inward/record.url?scp=80051671472&partnerID=8YFLogxK
U2 - 10.1016/j.jmb.2011.06.048
DO - 10.1016/j.jmb.2011.06.048
M3 - Article
SN - 0022-2836
VL - 411
SP - 1072
EP - 1082
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 5
ER -