1svj: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1svj.gif|left|200px]] | [[Image:1svj.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1svj", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_1svj| PDB=1svj | SCENE= }} | |||
}} | |||
'''The solution structure of the nucleotide binding domain of KdpB''' | '''The solution structure of the nucleotide binding domain of KdpB''' | ||
Line 31: | Line 28: | ||
[[Category: Haupt, M.]] | [[Category: Haupt, M.]] | ||
[[Category: Kessler, H.]] | [[Category: Kessler, H.]] | ||
[[Category: | [[Category: Alpha-beta sandwich]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:11:04 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 09:11, 3 May 2008
The solution structure of the nucleotide binding domain of KdpB
OverviewOverview
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 StructureAbout this Structure
1SVJ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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