3CGA

Crystal structure of metastasis-associated protein S100A4 in the active, calcium-bound form

Summary for 3CGA

• Entry DOI: 10.2210/pdb3cga/pdb
• Descriptor: Protein S100-A4, CALCIUM ION (3 entities in total)
• Functional Keywords: calcium-binding, metal binding protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 23651.39

Authors

Pathuri, P.,Luecke, H. (deposition date: 2008-03-05, release date: 2008-09-30, Last modification date: 2024-02-21)

Primary citation

Pathuri, P.,Vogeley, L.,Luecke, H.
Crystal structure of metastasis-associated protein S100A4 in the active calcium-bound form
J.Mol.Biol., 383:62-77, 2008

PubMed Abstract: S100A4 (metastasin) is a member of the S100 family of calcium-binding proteins that is directly involved in tumorigenesis. Until recently, the only structural information available was the solution NMR structure of the inactive calcium-free form of the protein. Here we report the crystal structure of human S100A4 in the active calcium-bound state at 2.03 A resolution that was solved by molecular replacement in the space group P6(5) with two molecules in the asymmetric unit from perfectly merohedrally twinned crystals. The Ca(2+)-bound S100A4 structure reveals a large conformational change in the three-dimensional structure of the dimeric S100A4 protein upon calcium binding. This calcium-dependent conformational change opens up a hydrophobic binding pocket that is capable of binding to target proteins such as annexin A2, the tumor-suppressor protein p53 and myosin IIA. The structure of the active form of S100A4 provides insight into its interactions with its binding partners and a better understanding of its role in metastasis.

PubMed: 18783790
DOI: 10.1016/j.jmb.2008.04.076

Experimental method

X-RAY DIFFRACTION (2.03 Å)