NMR solution structure of calerythrin, an EF-hand calcium-binding protein from Saccharopolyspora erythraea.
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.
Tossavainen
Helena
H
NMR laboratory, Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, Finland.
Permi
Perttu
P
Annila
Arto
A
Kilpeläinen
Ilkka
I
Drakenberg
Torbjörn
T
D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins; D002118:Calcium / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D002147:Calmodulin / Q000737:chemistry; D002816:Chordata, Nonvertebrate / Q000378:metabolism; D020832:EF Hand Motifs; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011077:Polychaeta / Q000378:metabolism; D011487:Protein Conformation; D016930:Saccharopolyspora / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D002135:Calcium-Binding Proteins; D002147:Calmodulin; C090958:calerythrin protein, Saccharopolyspora erythraea; D002118:Calcium