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 stability of the coiled-coil structure near to N-terminus influence the heat resistance of harpin proteins from Xanthomonas.

BMC microbiology - 12 Nov 2020

Liu Yue, Zhou Xiaoyun, Liu Wenbo, Miao Weiguo

Abstract excerpt

BACKGROUND: Heat resistance is a common characteristic of harpins, a class of proteins found in Gram-negative bacteria, which may be related to the stability of coiled-coil (CC) structure. The CC structure is a ubiquitous protein folding and assembly motif made of α-helices wrapping around each other forming a supercoil. Specifically, whether the stability of the CC structure near to N-terminus of four selected...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Bacterial Outer Membrane Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hot Temperature

Share to Nicotiana

Share to Plant Diseases

Share to Protein Structure, Secondary

Share to Protein Structure, Tertiary

Share to Xanthomonas

Source

Open in PubMed Open full text

Identifiers

PMID: 33183263
DOI: 10.1186/s12866-020-02029-6
PMCID: PMC7663895

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The stability of the coiled-coil structure near to N-terminus influence the heat resistance of harpin proteins from Xanthomonas.PMID 33183263Read ↗

HpaXpm, a novel harpin of Xanthomonas phaseoli pv. manihotis, acts as an elicitor with high thermal stability, reduces disease, and promotes plant growth.Semantic proximity Read ↗

Mutations in the N-terminal coding region of the harpin protein Hpa1 from Xanthomonas oryzae cause loss of hypersensitive reaction induction in tobacco.Semantic proximity Read ↗

A highly-conserved single-stranded DNA-binding protein in Xanthomonas functions as a harpin-like protein to trigger plant immunity.Semantic proximity Read ↗

Functional characterization and transcriptional analysis of degQ of Xanthomonas campestris pathovar campestris.Semantic proximity Read ↗

Evolutionary analysis of prokaryotic heat-shock transcription regulatory protein σ³².Semantic proximity Read ↗

Functional characterization of the type III secretion ATPase HrcN from the plant pathogen Xanthomonas campestris pv. vesicatoria.Semantic proximity Read ↗

Structural requirements of the phytoplasma effector protein SAP54 for causing homeotic transformation of floral organsSemantic proximity Read ↗

Structural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity.Semantic proximity Read ↗

Structure of the HopA1(21-102)-ShcA chaperone-effector complex of Pseudomonas syringae reveals conservation of a virulence factor binding motif from animal to plant pathogens.Semantic proximity Read ↗

Remarkable improvement in the heat stability of CutA1 from Escherichia coli by rational protein design.Semantic proximity Read ↗

Identification of specific fragments of HpaG Xooc, a harpin from Xanthomonas oryzae pv. oryzicola, that induce disease resistance and enhance growth in plants.Semantic proximity Read ↗

Involvement of the Heat Shock Protein HtpG of Salmonella Typhimurium in Infection and Proliferation in HostsSemantic proximity Read ↗

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