1M39

Solution structure of the C-terminal fragment (F86-I165) of the human centrin 2 in calcium saturated form

Summary for 1M39

• Entry DOI: 10.2210/pdb1m39/pdb
• NMR Information: BMRB: 5503
• Descriptor: Caltractin, isoform 1 (1 entity in total)
• Functional Keywords: ef-hand, cell cycle
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton, centrosome, centriole: P41208
• Total number of polymer chains: 1
• Total formula weight: 10390.69

Authors

Matei, E.,Miron, S.,Blouquit, Y.,Duchambon, P.,Durussel, P.,Cox, J.A.,Craescu, C.T. (deposition date: 2002-06-27, release date: 2003-03-25, Last modification date: 2024-05-22)

Primary citation

Matei, E.,Miron, S.,Blouquit, Y.,Duchambon, P.,Durussel, P.,Cox, J.A.,Craescu, C.T.
C-terminal half of human centrin 2 behaves like a regulatory EF-hand domain
Biochemistry, 42:1439-1450, 2003

PubMed Abstract: Human centrin 2 (HsCen2) is an EF-hand protein that plays a critical role in the centrosome duplication and separation during cell division. We studied the structural and Ca(2+)-binding properties of two C-terminal fragments of this protein: SC-HsCen2 (T94-Y172), covering two EF-hands, and LC-HsCen2 (M84-Y172), having 10 additional residues. Both fragments are highly disordered in the apo state but become better structured (although not conformationally homogeneous) in the presence of Ca(2+) and depending on the nature of the cations (K(+) or Na(+)) in the buffer. Only the longer C-terminal domain, in the Ca(2+)-saturated state and in the presence of Na(+) ions, was amenable to structure determination by nuclear magnetic resonance. The solution structure of LC-HsCen2 reveals an open two EF-hand structure, similar to the conformation of related Ca(2+)-saturated regulatory domains. Unexpectedly, the N-terminal helix segment (F86-T94) lies over the exposed hydrophobic cavity. This unusual intramolecular interaction increases considerably the Ca(2+) affinity and constitutes a useful model for the target binding.

PubMed: 12578356
DOI: 10.1021/bi0269714

Experimental method

SOLUTION NMR