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

Determinants for substrate specificity of the bacterial PP2C protein phosphatase tPphA from Thermosynechococcus elongatus.

The FEBS journal - 1 Jan 2013

Su Jiyong, Forchhammer Karl

Abstract excerpt

Members of the Mg(2+)- or Mn(2+)-dependent protein phosphatases/PP2C-like serine/threonine phosphatases (PPM/PP2C) are abundant and widely distributed in prokaryotes and eukaryotes, where they regulate diverse signal transduction pathways. Despite low sequence conservation, the structure of their catalytic core is highly conserved except for a flexible loop termed the flap subdomain. Bacterial PPM/PP2C members...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Crystallography, X-Ray
Share to Cyanobacteria

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

Share to Histidine

Share to Immunoblotting

Share to Phosphoprotein Phosphatases

Share to Phosphoproteins

Share to Protein Phosphatase 2C

Source

Identifiers

PMID: 22212593
DOI: 10.1111/j.1742-4658.2011.08466.x

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

Determinants for substrate specificity of the bacterial PP2C protein phosphatase tPphA from Thermosynechococcus elongatus.PMID 22212593Read ↗

Structural analysis of the PP2C phosphatase tPphA from Thermosynechococcus elongatus: a flexible flap subdomain controls access to the catalytic site.Semantic proximity Read ↗

A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo.Semantic proximity Read ↗

Metal-dependent Ser/Thr protein phosphatase PPM family: Evolution, structures, diseases and inhibitors.Semantic proximity Read ↗

Mechanism of the phosphatase component of Clostridium thermocellum polynucleotide kinase-phosphatase.Semantic proximity Read ↗

The beta12-beta13 loop is a key regulatory element for the activity and properties of the catalytic domain of protein phosphatase 1 and 2B.Semantic proximity Read ↗

Distinct enzymic functional groups are required for the phosphomonoesterase and phosphodiesterase activities of Clostridium thermocellum polynucleotide kinase/phosphatase.Semantic proximity Read ↗

A trapped human PPM1A-phosphopeptide complex reveals structural features critical for regulation of PPM protein phosphatase activity.Semantic proximity Read ↗

Genome-wide survey of prokaryotic O-protein phosphatases.Semantic proximity Read ↗

Methylation of the C-terminal leucine residue of the PP2A catalytic subunit is unnecessary for the catalytic activity and the binding of regulatory subunit (PR55/B).Semantic proximity Read ↗

The histidine phosphatase superfamily: structure and functionSemantic proximity Read ↗

A novel signal transduction protein P(II) variant from Synechococcus elongatus PCC 7942 indicates a two-step process for NAGK-P(II) complex formation.Semantic proximity Read ↗

Structural basis for the preference of the Arabidopsis thaliana phosphatase RLPH2 for tyrosine-phosphorylated substrates.Semantic proximity Read ↗

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