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Prokaryotic Kdp-ATPase: Recent Insights into the Structure and Function of KdpB

Haupt M.a · Bramkamp M.b · Coles M.a, c · Kessler H.a · Altendorf K.b

Author affiliations

aInstitut für Organische Chemie und Biochemie, Technische Universität München, Garching, bUniversität Osnabrück, Fachbereich Biologie/Chemie, Abteilung Mikrobiologie, Osnabrück, and cMax Planck Institut für Entwicklungsbiologie, Tübingen, Germany

Related Articles for ""

J Mol Microbiol Biotechnol 2005;10:120–131

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Article / Publication Details

First-Page Preview
Abstract of Minireview

Published online: April 27, 2006
Issue release date: April 2006

Number of Print Pages: 12
Number of Figures: 8
Number of Tables: 0

ISSN: 1464-1801 (Print)
eISSN: 1660-2412 (Online)

For additional information: http://www.karger.com/MMB

Abstract

P-type ATPases are amongst the most abundant enzymes that are responsible for active transport of ions across biological membranes. Within the last 5 years a detailed picture of the structure and function of these transport ATPases has emerged. Here, we report on the recent progress in elucidating the molecular mechanism of a unique, prokaryotic member of P-type ATPases, the Kdp-ATPase. The review focuses on the catalytic parts of the central subunit, KdpB. The structure of the nucleotide-binding domain was solved by NMR spectroscopy at high resolution and a model of the nucleotide-binding mode was presented. The nucleotide turned out to be ‘clipped’ into the binding pocket by a π-π interaction to F377 on one side and a cation-π interaction to K395 on the other. The 395KGXXD/E motif and thus the nucleotide-binding mode seems to be conserved in all P-type ATPases, except the heavy metal-transporting (class IB) ATPases. Hence, it can be concluded that KdpB is currently misgrouped as class IA. Mutational studies on two highly conserved residues (D583 and K586) in the transmembrane helix 5 of KdpB revealed that they are indispensable in coupling ATP hydrolysis to ion translocation. Based on these results, two possible pathways for the reaction cycle are discussed.

© 2005 S. Karger AG, Basel


Article / Publication Details

First-Page Preview
Abstract of Minireview

Published online: April 27, 2006
Issue release date: April 2006

Number of Print Pages: 12
Number of Figures: 8
Number of Tables: 0

ISSN: 1464-1801 (Print)
eISSN: 1660-2412 (Online)

For additional information: http://www.karger.com/MMB


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