Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The nucleotide-binding domain of the Zn2+-transporting P-type ATPase from Escherichia coli carries a glycine motif that may be involved in binding of ATP.

The Biochemical journal - 1 Jan 2004

Okkeri Juha, Laakkonen Liisa, Haltia Tuomas

Abstract excerpt

In P-type ATPases, the nucleotide-binding (N) domain is located in the middle of the sequence which folds into the phosphorylation (P) domain. The N domain of ZntA, a Zn2+-translocating P-type ATPase from Escherichia coli, is approx. 13% identical with the N domain of sarcoplasmic reticulum Ca2+-ATPase. None of the Ca2+-ATPase residues involved in binding of ATP are found in ZntA. However, the sequence...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Triphosphatases
Share to Adenosine Triphosphate

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

Share to Amino Acid Motifs

Share to Glycine

Share to Histidine

Share to Kinetics

Share to Nucleotides

Source

Open in PubMed Open full text

Identifiers

PMID: 14510639
DOI: 10.1042/BJ20030740
PMCID: PMC1223847

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The nucleotide-binding domain of the Zn2+-transporting P-type ATPase from Escherichia coli carries a glycine motif that may be involved in binding of ATP.PMID 14510639Read ↗

Introducing Wilson disease mutations into the zinc-transporting P-type ATPase of Escherichia coli. The mutation P634L in the 'hinge' motif (GDGXNDXP) perturbs the formation of the E2P state.Semantic proximity Read ↗

Identification and analysis of 21 novel disease-causing amino acid substitutions in the conserved part of ATP7A.Semantic proximity Read ↗

The hydrogen bonds between Arg423 and Glu472 and other key residues, Asp443, Ser477, and Pro489, are responsible for the formation and a different positioning of TNP-ATP and ATP within the nucleotide-binding site of Na(+)/K(+)-ATPase.Semantic proximity Read ↗

The P-loop--a common motif in ATP- and GTP-binding proteins.Semantic proximity Read ↗

Role of conserved TGDGVND-loop in Mg2+ binding, phosphorylation, and energy transfer in Na,K-ATPase.Semantic proximity Read ↗

Functional consequences of alterations to amino acids at the M5S5 boundary of the Ca(2+)-ATPase of sarcoplasmic reticulum. Mutation Tyr763-->Gly uncouples ATP hydrolysis from Ca2+ transport.Semantic proximity Read ↗

Critical role of a transmembrane lysine in aminophospholipid transport by mammalian photoreceptor P4-ATPase ATP8A2.Semantic proximity Read ↗

Roles of conserved P domain residues and Mg2+ in ATP binding in the ground and Ca2+-activated states of sarcoplasmic reticulum Ca2+-ATPase.Semantic proximity Read ↗

A Highly Conserved Glycine in a Hotspot for Neurological Disease Mutations in Na+,K+-ATPase Is Critical to Na+ and K+ Occlusion.Semantic proximity Read ↗

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

The amino acid sequence 442GDASE446 in Na/K-ATPase is an important motif in forming the high and low affinity ATP binding pockets.Semantic proximity Read ↗

Catalytic and regulatory sites of yeast plasma membrane H(+)-ATPase studied by directed mutagenesis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.