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Article

The holo-form of the nucleotide binding domain of the KdpFABC complex from Escherichia coli reveals a new binding mode.

The Journal of biological chemistry - 7 Apr 2006

Haupt Melina, Bramkamp Marc, Heller Markus, Coles Murray, Deckers-Hebestreit Gabriele, Herkenhoff-Hesselmann Brigitte, Altendorf Karlheinz, Kessler Horst

Abstract excerpt

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...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 16354672
DOI: 10.1074/jbc.M508290200

Genes

PNP

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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