1DEG

THE LINKER OF DES-GLU84 CALMODULIN IS BENT AS SEEN IN THE CRYSTAL STRUCTURE

Summary for 1DEG

• Entry DOI: 10.2210/pdb1deg/pdb
• Descriptor: CALMODULIN, CALCIUM ION (2 entities in total)
• Functional Keywords: calcium-binding protein
• Biological source: Bos taurus (cattle)
• Cellular location: Cytoplasm, cytoskeleton, spindle: P02593
• Total number of polymer chains: 1
• Total formula weight: 16194.93

Authors

Raghunathan, S.,Chandross, R.,Cheng, B.P.,Persechini, A.,Sobottk, S.E.,Kretsinger, R.H. (deposition date: 1993-06-07, release date: 1994-05-31, Last modification date: 2024-02-07)

Primary citation

Raghunathan, S.,Chandross, R.J.,Cheng, B.P.,Persechini, A.,Sobottka, S.E.,Kretsinger, R.H.
The linker of des-Glu84-calmodulin is bent.
Proc.Natl.Acad.Sci.Usa, 90:6869-6873, 1993

PubMed Abstract: The crystal structure of a mutant calmodulin (CaM) lacking Glu-84 has been refined to R = 0.23 using data measured to 2.9-A resolution. In native CaM the central helix is fully extended, and the molecule is dumbbell shaped. In contrast, the deletion of Glu-84 causes a bend of 95 degrees in the linker region of the central helix at Ile-85. However, EF-hand domains 1 and 2 (lobe 1,2) do not touch lobe 3,4. The length, by alpha-carbon separation, of des-Glu84-CaM is 56 A; that of native CaM is 64 A. The shape of des-Glu84-CaM is similar to that of native CaM, as it is bound to the target peptide of myosin light-chain kinase. This result supports the proposal that the linker region of the central helix of CaM functions as a flexible tether.

PubMed: 8341712
DOI: 10.1073/pnas.90.14.6869

Experimental method

X-RAY DIFFRACTION (2.9 Å)