Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of calerythrin, a prokaryotic 20 kDa calcium-binding protein has been determined by solution NMR spectroscopy. Distance, dihedral angle, J coupling, secondary chemical shift, residual dipolar coupling and radius of gyration restraints reveal four EF-hand motifs arranged in a compact globular structure. A tight turn in the middle of the amino acid sequence brings the two halves, each comprising a pair of EF-hands, close together. The structural similarity between calerythrin and the eukaryotic sarcoplasmic calcium-binding proteins is notable.
NMR solution structure of calerythrin, an EF-hand calcium-binding protein from Saccharopolyspora erythraea.,Tossavainen H, Permi P, Annila A, Kilpelainen I, Drakenberg T Eur J Biochem. 2003 Jun;270(11):2505-12. PMID:12755706[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tossavainen H, Permi P, Annila A, Kilpelainen I, Drakenberg T. NMR solution structure of calerythrin, an EF-hand calcium-binding protein from Saccharopolyspora erythraea. Eur J Biochem. 2003 Jun;270(11):2505-12. PMID:12755706
