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1FW4

CRYSTAL STRUCTURE OF E. COLI FRAGMENT TR2C FROM CALMODULIN TO 1.7 A RESOLUTION

Replaces:  1TRC
Summary for 1FW4
Entry DOI10.2210/pdb1fw4/pdb
DescriptorCALMODULIN, CALCIUM ION (3 entities in total)
Functional Keywordsef-hand, helix-loop-helix, fragment, calcium, tr2c, c-terminal domain, calmodulin, metal binding protein
Biological sourceBos taurus (cattle)
Cellular locationCytoplasm: P62157
Total number of polymer chains1
Total formula weight8235.98
Authors
Olsson, L.-L.,Sjolin, L. (deposition date: 2000-09-21, release date: 2001-05-02, Last modification date: 2023-08-09)
Primary citationOlsson, L.L.,Sjolin, L.
Structure of Escherichia coli fragment TR2C from calmodulin to 1.7 A resolution.
Acta Crystallogr.,Sect.D, 57:664-669, 2001
Cited by
PubMed Abstract: Fragment TR2C is the C-terminal part of the calcium-binding protein calmodulin, including residues 78-148. The crystal structure of TR2C was solved by molecular replacement and refined to a conventional R value of 21.8% (R(free) = 22.0%), using all data in the resolution range 20.0-1.7 A. This study shows that the secondary structure of TR2C, a pair of EF-hand motifs with two calcium-binding sites, is similar to the corresponding motifs in intact calmodulin. However, it also indicates that the N-terminus of helix E is closer to the C-terminus of helix H in TR2C than in the intact protein and that the loop connecting the EF-hands shows different conformations in the two structures. The crystal structure of TR2C was further found to be similar to the set of NMR structures of this fragment, although some pronounced differences exist.
PubMed: 11320306
DOI: 10.1107/S090744490100347X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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