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

Substitution of asparagine 76 by a tyrosine residue induces domain swapping in Helicobacter pylori phosphopantetheine adenylyltransferase.

Journal of biomolecular structure & dynamics - 1 Jan 2012

Cheng Chao-Sheng, Chen Wen-Ting, Chen Yu-Wen, Chen Chih-Hao, Luo Yong-Chun, Lyu Ping-Chiang, Yin Hsien-Sheng

Abstract excerpt

Phosphopantetheine adenylyltransferase (PPAT) catalyses the penultimate step in coenzyme A biosynthesis in bacteria and is therefore a candidate target for antibacterial drug development. We randomly mutated the residues in the Helicobacter pylori PPAT sequence to identify those that govern protein folding and ligand binding, and we describe the crystal structure of one of these mutants (I4V/N76Y) that contains...

Read the complete abstract on PubMed

Topics

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

Share to Asparagine
Share to Coenzyme A

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Helicobacter pylori

Share to Hydrogen Bonding

Share to Hydrophobic and Hydrophilic Interactions

Share to Nucleotidyltransferases

Share to Protein Subunits

Share to Tyrosine

Source

Identifiers

PMID: 22694317
DOI: 10.1080/07391102.2012.682213

Genes

PPAT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Substitution of asparagine 76 by a tyrosine residue induces domain swapping in Helicobacter pylori phosphopantetheine adenylyltransferase.PMID 22694317Read ↗

A remote surface loop modulates core structure and cold activity in phosphopantetheine adenylyltransferase.Semantic proximity Read ↗

Structural variation and inhibitor binding in polypeptide deformylase from four different bacterial speciesSemantic proximity Read ↗

The activity and stability of a cold-active acylaminoacyl peptidase rely on its dimerization by domain swapping.Semantic proximity Read ↗

Experimental evolution of adenylate kinase reveals contrasting strategies toward protein thermostability.Semantic proximity Read ↗

A Single Mutation in the "DSL" Motif of the Acyl Carrier Protein Can Prevent Its In Vivo Phosphopantetheinylation by E. coli Holo-Acyl Carrier Protein Synthase (AcpS).Semantic proximity Read ↗

Structural analysis of the bacterial HPr kinase/phosphorylase V267F mutant gives insights into the allosteric regulation mechanism of this bifunctional enzyme.Semantic proximity Read ↗

Role of the αC-β4 loop in protein kinase structure and dynamics.Semantic proximity Read ↗

PBP active site flexibility as the key mechanism for beta-lactam resistance in pneumococci.Semantic proximity Read ↗

A Single Amino Acid Change in the Response Regulator PhoP, Acquired during Yersinia pestis Evolution, Affects PhoP Target Gene Transcription and Polymyxin B Susceptibility.Semantic proximity Read ↗

Specific Mutations Reverse Regulatory Effects of Adenosine Phosphates and Increase Their Binding Stoichiometry in CBS Domain-Containing Pyrophosphatase.Semantic proximity Read ↗

The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases.Semantic proximity Read ↗

Conformational response to ligand binding in phosphomannomutase2: insights into inborn glycosylation disorder.Semantic proximity Read ↗

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