Motion in Glucose ABC transporter ATPase subunit [glcv]

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Classification [D-h-2]

1oxs nucleotide-free
1oxt nucleotide-free
1oxu nucleotide-bound
1oxv nucleotide-bound

From the abstract to Verdon et al. JMB 330:343-58: "Comparisons of the nucleotide-free and nucleotide-bound structures of GlcV reveal re-orientations of the ABCalpha subdomain and the C-terminal domain relative to the ABCalpha/beta subdomain, and switch-like rearrangements in the P-loop and Q-loop regions. Additionally, large conformational differences are observed between the GlcV structures and those of other ABC-ATPases, further emphasizing the inherent flexibility of these proteins. Notably, a comparison of the monomeric AMPPNP-Mg(2+)-bound GlcV structure with that of the dimeric ATP-Na(+)-bound LolD-E171Q mutant reveals a +/-20 degrees rigid body re-orientation of the ABCalpha subdomain relative to the ABCalpha/beta subdomain, accompanied by a local conformational difference in the Q-loop."

Verdon, G., Albers, S. V., Dijkstra, B. W., Driessen, A. J., Thunnissen, A. M. (2003). Crystal Structures of the ATPase Subunit of the Glucose Abc Transporter from Sulfolobus Solfataricus: Nucleotide-Free and Nucleotide-Bound Conformations J.Mol.Biol. 330 pp. 343 [Medline info for 12823973]

GO terms associated with structures
Molecular functionnucleoside-triphosphatase activity, nucleotide binding, ATP binding, ATPase activity


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Best representative
Morph Morph name Structure #1 Structure #2 Residues
Glcv 1oxs [ C ] 1oxu [ C ] 353

User-submitted morphs
Morph Morph name Structure #1 Structure #2 Residues
021420-11481 Glcv 1oxs [ C ] 1oxt [ A ] 353

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_