Motion in ATP-binding cassette protein MalK [malk]
[ jump to morphs ]
Classification [S-n-2]
Description From Chen et al. (Mol Cell. 2003 Sep;12(3):651-61.): "In the two nucleotide-free structures, the N-terminal nucleotide binding domains are separated to differing degrees, and the dimer is maintained through contacts of the C-terminal regulatory domains. In the ATP-bound form, the nucleotide binding domains make contact and two ATPs lie buried along the dimer interface. The two nucleotide binding domains of the dimer open and close like a pair of tweezers."
Morphs
[ show all images ]
Best representative Morph Morph name Structure #1 Structure #2 Residues [ ] [ ]
Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu