1LKJ

NMR Structure of Apo Calmodulin from Yeast Saccharomyces cerevisiae

Summary for 1LKJ

• Entry DOI: 10.2210/pdb1lkj/pdb
• Related: 1F54 1F55
• NMR Information: BMRB: 5353
• Descriptor: Calmodulin (1 entity in total)
• Functional Keywords: yeast calmodulin, saccharomyces cerevisiae, ef-hand, metal binding protein
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm, cytoskeleton, spindle pole body: P06787
• Total number of polymer chains: 1
• Total formula weight: 16016.60

Authors

Ishida, H.,Nakashima, K.,Kumaki, Y.,Nakata, M.,Hikichi, K.,Yazawa, M. (deposition date: 2002-04-25, release date: 2003-04-29, Last modification date: 2024-05-29)

Primary citation

Ishida, H.,Nakashima, K.,Kumaki, Y.,Nakata, M.,Hikichi, K.,Yazawa, M.
The solution structure of apocalmodulin from Saccharomyces cerevisiae implies a mechanism for its unique Ca2+ binding property.
Biochemistry, 41:15536-15542, 2002

PubMed Abstract: We have determined the solution structure of calmodulin (CaM) from yeast (Saccharomyces cerevisiae) (yCaM) in the apo state by using NMR spectroscopy. yCaM is 60% identical in its amino acid sequence with other CaMs, and exhibits its unique biological features. yCaM consists of two similar globular domains (N- and C-domain) containing three Ca(2+)-binding motifs, EF-hands, in accordance with the observed 3 mol of Ca(2+) binding. In the solution structure of yCaM, the conformation of the N-domain conforms well to the one of the expressed N-terminal half-domains of yCaM [Ishida, H., et al. (2000) Biochemistry 39, 13660-13668]. The conformation of the C-domain basically consists of a pair of helix-loop-helix motifs, though a segment corresponding to the forth Ca(2+)-binding site of CaM deviates in its primary structure from a typical EF-hand motif and loses the ability to bind Ca(2+). Thus, the resulting conformation of each domain is essentially identical to the corresponding domain of CaM in the apo state. A flexible linker connects the two domains as observed for CaM. Any evidence for the previously reported interdomain interaction in yCaM was not observed in the solution structure of the apo state. Hence, the interdomain interaction possibly occurs in the course of Ca(2+) binding and generates a cooperative Ca(2+) binding among all three sites. Preliminary studies on a mutant protein of yCaM, E104Q, revealed that the Ca(2+)-bound N-domain interacts with the apo C-domain and induces a large conformational change in the C-domain.

PubMed: 12501182
DOI: 10.1021/bi020330r

Experimental method

SOLUTION NMR