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NMR solution structure of calerythrin, an EF-hand calcium-binding protein from Saccharopolyspora erythraea
- Tossavainen, H (author)
- Permi, P (author)
- Annila, A (author)
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- Kilpelainen, I (author)
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- (creator_code:org_t)
- Wiley, 2003
- 2003
- English.
- In: European Journal of Biochemistry. - : Wiley. - 0014-2956 .- 1432-1033. ; 270:11, s. 2505-2512
- Journal article (peer-reviewed)
Abstract
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- 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.
Subject headings
- NATURVETENSKAP -- Kemi -- Fysikalisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Physical Chemistry (hsv//eng)
Keyword
- calcium-binding
- calerythrin
- NMR
- structure
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- art (subject category)
- ref (subject category)
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- Permi, P
- Annila, A
- Kilpelainen, I
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- Lund University
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