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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nya ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nya ConSurf]. | ||
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== 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<ref>PMID:12755706</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Latest revision as of 08:55, 22 May 2024
NMR SOLUTION STRUCTURE OF CALERYTHRIN, AN EF-HAND CALCIUM-BINDING PROTEIN
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