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

Crystal structure of alkaline phosphatase from the Antarctic bacterium TAB5.

Journal of molecular biology - 2 Mar 2007

Wang Ellen, Koutsioulis Dimitris, Leiros Hanna-Kirsti S, Andersen Ole Andreas, Bouriotis Vassilis, Hough Edward, Heikinheimo Pirkko

Abstract excerpt

Alkaline phosphatases (APs) are non-specific phosphohydrolases that are widely used in molecular biology and diagnostics. We describe the structure of the cold active alkaline phosphatase from the Antarctic bacterium TAB5 (TAP). The fold and the active site geometry are conserved with the other AP structures, where the monomer has a large central beta-sheet enclosed by alpha-helices. The dimer interface of TAP is...

Read the complete abstract on PubMed

Topics

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

Share to Alkaline Phosphatase
Share to Bacteria

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

Share to Binding Sites

Share to Crystallization

Share to Crystallography, X-Ray

Share to Metals

Share to Protein Structure, Tertiary

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 17198711
DOI: 10.1016/j.jmb.2006.11.079

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

Crystal structure of alkaline phosphatase from the Antarctic bacterium TAB5.PMID 17198711Read ↗

Directed evolution on the cold adapted properties of TAB5 alkaline phosphatase.Semantic proximity Read ↗

Coordination sphere of the third metal site is essential to the activity and metal selectivity of alkaline phosphatases.Semantic proximity Read ↗

Structural and functional characterization of a cold-adapted stand-alone TPM domain reveals a relationship between dynamics and phosphatase activity.Semantic proximity Read ↗

The histidine phosphatase superfamily: structure and functionSemantic proximity Read ↗

Engineered disulfide bonds increase active-site local stability and reduce catalytic activity of a cold-adapted alkaline phosphatase.Semantic proximity Read ↗

Structural evidence of functional divergence in human alkaline phosphatases.Semantic proximity Read ↗

Divergence of structure and function in the haloacid dehalogenase enzyme superfamily: Bacteroides thetaiotaomicron BT2127 is an inorganic pyrophosphatase.Semantic proximity Read ↗

Identification of rare slipknots in proteins and their implications for stability and folding.Semantic proximity Read ↗

Structural and functional analysis of the phosphoryl transfer reaction mediated by the human small C-terminal domain phosphatase, Scp1.Semantic proximity Read ↗

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

Structural characterization of the catalytic calcium-binding site in diisopropyl fluorophosphatase (DFPase)--comparison with related beta-propeller enzymes.Semantic proximity Read ↗

Bacillus subtilis alkaline phosphatases III and IV. Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure.Semantic proximity Read ↗

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