2a29: Difference between revisions

Revision as of 04:23, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2a29.png

Template:STRUCTURE 2a29

The solution structure of the AMP-PNP bound nucleotide binding domain of KdpBThe solution structure of the AMP-PNP bound nucleotide binding domain of KdpB

Template:ABSTRACT PUBMED 16354672

About this StructureAbout this Structure

2A29 is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1x6k. Full experimental information is available from OCA.

ReferenceReference

The holo-form of the nucleotide binding domain of the KdpFABC complex from Escherichia coli reveals a new binding mode., Haupt M, Bramkamp M, Heller M, Coles M, Deckers-Hebestreit G, Herkenhoff-Hesselmann B, Altendorf K, Kessler H, J Biol Chem. 2006 Apr 7;281(14):9641-9. Epub 2005 Dec 14. PMID:16354672

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''The solution structure of the AMP-PNP bound nucleotide binding domain of KdpB'''
+===The solution structure of the AMP-PNP bound nucleotide binding domain of KdpB===
-==Overview==
+<!--
-P-type ATPases are ubiquitously abundant enzymes involved in active transport of charged residues across biological membranes. The KdpB subunit of the prokaryotic Kdp-ATPase (KdpFABC complex) shares characteristic regions of homology with class II-IV P-type ATPases and has been shown previously to be misgrouped as a class IA P-type ATPase. Here, we present the NMR structure of the AMP-PNP-bound nucleotide binding domain KdpBN of the Escherichia coli Kdp-ATPase at high resolution. The aromatic moiety of the nucleotide is clipped into the binding pocket by Phe(377) and Lys(395) via a pi-pi stacking and a cation-pi interaction, respectively. Charged residues at the outer rim of the binding pocket (Arg(317), Arg(382), Asp(399), and Glu(348)) stabilize and direct the triphosphate group via electrostatic attraction and repulsion toward the phosphorylation domain. The nucleotide binding mode was corroborated by the replacement of critical residues. The conservative mutation F377Y produced a high residual nucleotide binding capacity, whereas replacement by alanine resulted in low nucleotide binding capacities and a considerable loss of ATPase activity. Similarly, mutation K395A resulted in loss of ATPase activity and nucleotide binding affinity, even though the protein was properly folded. We present a schematic model of the nucleotide binding mode that allows for both high selectivity and a low nucleotide binding constant, necessary for the fast and effective turnover rate realized in the reaction cycle of the Kdp-ATPase.
+The line below this paragraph, {{ABSTRACT_PUBMED_16354672}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16354672}}
 ==About this Structure==
-A29 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1x6k 1x6k]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A29 OCA].
+A29 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1x6k 1x6k]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A29 OCA].
 ==Reference==
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 [[Category: Kessler, H.]]
 [[Category: Alpha-beta sandwich]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:30:46 2008''
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