1svj
From Proteopedia
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'''The solution structure of the nucleotide binding domain of KdpB''' | '''The solution structure of the nucleotide binding domain of KdpB''' | ||
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[[Category: Haupt, M.]] | [[Category: Haupt, M.]] | ||
[[Category: Kessler, H.]] | [[Category: Kessler, H.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:11:04 2008'' | |
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Revision as of 06:11, 3 May 2008
The solution structure of the nucleotide binding domain of KdpB
Overview
P-type ATPases are involved in the active transport of ions across biological membranes. The KdpFABC complex (P-type ATPase) of Escherichia coli is a high-affinity K+ uptake system that operates only when the cell experiences osmotic stress or K+ limitation. Here, we present the solution structure of the nucleotide binding domain of KdpB (backbone RMSD 0.17 A) and a model of the AMP-PNP binding mode based on intermolecular distance restraints. The calculated AMP-PNP binding mode shows the purine ring of the nucleotide to be "clipped" into the binding pocket via a pi-pi-interaction to F377 on one side and a cation-pi-interaction to K395 on the other. This binding mechanism seems to be conserved in all P-type ATPases, except the heavy metal transporting ATPases (type IB). Thus, we conclude that the Kdp-ATPase (currently type IA) is misgrouped and has more similarities to type III ATPases. The KdpB N-domain is the smallest and simplest known for a P-type ATPase, and represents a minimal example of this functional unit. No evidence of significant conformational changes was observed within the N-domain upon nucleotide binding, thus ruling out a role for ATP-induced conformational changes in the reaction cycle.
About this Structure
1SVJ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Inter-domain motions of the N-domain of the KdpFABC complex, a P-type ATPase, are not driven by ATP-induced conformational changes., Haupt M, Bramkamp M, Coles M, Altendorf K, Kessler H, J Mol Biol. 2004 Oct 1;342(5):1547-58. PMID:15364580 Page seeded by OCA on Sat May 3 09:11:04 2008
