1svj: Difference between revisions
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Potassium-transporting_ATPase Potassium-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.12 3.6.3.12] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Potassium-transporting_ATPase Potassium-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.12 3.6.3.12] </span> | ||
|GENE= KDPB, B0697 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= KDPB, B0697 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1u7q|1U7Q]], [[1x6k|1X6K]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1svj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svj OCA], [http://www.ebi.ac.uk/pdbsum/1svj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1svj RCSB]</span> | |||
}} | }} | ||
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[[Category: alpha-beta sandwich]] | [[Category: alpha-beta sandwich]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:47:30 2008'' | ||
Revision as of 23:47, 30 March 2008
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| Gene: | KDPB, B0697 (Escherichia coli) | ||||||
| Activity: | Potassium-transporting ATPase, with EC number 3.6.3.12 | ||||||
| Related: | 1U7Q, 1X6K
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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