1B4C

SOLUTION STRUCTURE OF RAT APO-S100B USING DIPOLAR COUPLINGS

Summary for 1B4C

• Entry DOI: 10.2210/pdb1b4c/pdb
• NMR Information: BMRB: 5544
• Descriptor: PROTEIN (S-100 PROTEIN, BETA CHAIN) (1 entity in total)
• Functional Keywords: s100beta, s100b, dipolar couplings, ef-hand, s100 protein, calcium- binding protein, four-helix bundle, three-dimensional structure, solution structure, metal binding protein
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm (By similarity): P04631
• Total number of polymer chains: 2
• Total formula weight: 21516.10

Authors

Weber, D.J.,Drohat, A.C.,Tjandra, N.,Baldisseri, D.M. (deposition date: 1998-12-17, release date: 1998-12-30, Last modification date: 2024-05-22)

Primary citation

Drohat, A.C.,Tjandra, N.,Baldisseri, D.M.,Weber, D.J.
The use of dipolar couplings for determining the solution structure of rat apo-S100B(betabeta).
Protein Sci., 8:800-809, 1999

PubMed Abstract: The relative orientations of adjacent structural elements without many well-defined NOE contacts between them are typically poorly defined in NMR structures. For apo-S100B(betabeta) and the structurally homologous protein calcyclin, the solution structures determined by conventional NMR exhibited considerable differences and made it impossible to draw unambiguous conclusions regarding the Ca2+-induced conformational change required for target protein binding. The structure of rat apo-S100B(betabeta) was recalculated using a large number of constraints derived from dipolar couplings that were measured in a dilute liquid crystalline phase. The dipolar couplings orient bond vectors relative to a single-axis system, and thereby remove much of the uncertainty in NOE-based structures. The structure of apo-S100B(betabeta) indicates a minimal change in the first, pseudo-EF-hand Ca2+ binding site, but a large reorientation of helix 3 in the second, classical EF-hand upon Ca2+ binding.

PubMed: 10211826

Experimental method

SOLUTION NMR