1K09

Solution structure of BetaCore, A Designed Water Soluble Four-Stranded Antiparallel b-sheet Protein

Summary for 1K09

• Entry DOI: 10.2210/pdb1k09/pdb
• NMR Information: BMRB: 5183
• Descriptor: Core Module I, Core Module II, (7E)-4,9-dioxo-6-oxa-3,7,10-triazadodec-7-ene-1,12-dioic acid (3 entities in total)
• Functional Keywords: four-stranded antiparallel beta-sheet, de novo protein
• Biological source: Bos taurus (Bovine); More
• Cellular location: Secreted: P00974 P00974
• Total number of polymer chains: 2
• Total formula weight: 5967.91

Authors

Carulla, N.,Woodward, C.,Barany, G. (deposition date: 2001-09-18, release date: 2002-07-10, Last modification date: 2024-02-21)

Primary citation

Carulla, N.,Woodward, C.,Barany, G.
BetaCore, a designed water soluble four-stranded antiparallel beta-sheet protein.
Protein Sci., 11:1539-1551, 2002

PubMed Abstract: BetaCore is a designed approximately 50-residue protein in which two BPTI-derived core modules, CM I and CM II, are connected by a 22-atom cross-link. At low temperature and pH 3, homo- and heteronuclear NMR data report a dominant folded ('f') conformation with well-dispersed chemical shifts, i, i+1 periodicity, numerous long-range NOEs, and slowed amide hydrogen isotope exchange patterns that is a four-stranded antiparallel beta-sheet with nonsymmetrical and specific association of CM I and CM II. BetaCore 'f' conformations undergo reversible, global, moderately cooperative, non-two-state thermal transitions to an equilibrium ensemble of unfolded 'u' conformations. There is a significant energy barrier between 'f' and 'u' conformations. This is the first designed four-stranded antiparallel beta-sheet that folds in water.

PubMed: 12021452
DOI: 10.1110/ps.4440102

Experimental method

SOLUTION NMR