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CRYSTAL STRUCTURE OF E. COLI FRAGMENT TR2C FROM CALMODULIN TO 1.7 A RESOLUTIONCRYSTAL STRUCTURE OF E. COLI FRAGMENT TR2C FROM CALMODULIN TO 1.7 A RESOLUTION
Structural highlights
FunctionCALM_BOVIN Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CEP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedFragment 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. Structure of Escherichia coli fragment TR2C from calmodulin to 1.7 A resolution.,Olsson LL, Sjolin L Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):664-9. Epub 2001, Apr 24. PMID:11320306[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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