1svj: Difference between revisions

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[[Image:1svj.gif|left|200px]]
[[Image:1svj.gif|left|200px]]


{{Structure
<!--
|PDB= 1svj |SIZE=350|CAPTION= <scene name='initialview01'>1svj</scene>
The line below this paragraph, containing "STRUCTURE_1svj", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND=
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|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>
or leave the SCENE parameter empty for the default display.
|GENE= KDPB, B0697 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
-->
|DOMAIN=
{{STRUCTURE_1svj|  PDB=1svj |  SCENE= }}  
|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>
}}


'''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.]]
[[Category: alpha-beta sandwich]]
[[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 Sun Mar 30 23:47:30 2008''

Revision as of 09:11, 3 May 2008

File:1svj.gif

Template:STRUCTURE 1svj

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

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