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

How BamA recruits OMP substrates via poly-POTRAs domain.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology - 1 Dec 2019

Ma Xiaodan, Wang Qianqian, Li Yuwen, Tan Pan, Wu Haiyan, Wang Pengran, Dong Xue, Hong Liang, Meng Guoyu

Abstract excerpt

Almost all the outer membrane proteins (OMPs) fold into an invariant β-barrel fold via the polypeptide-transport-associated (POTRA) motif and β-barrel assembly machinery (BAM). However, whether and how poly-POTRAs interact with OMPs remain largely unknown. Here, we have characterized the structures of Haemophilus influenzae poly-POTRAs via X-ray crystallography, small angle X-ray scattering, and molecular...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Outer Membrane Proteins
Share to Conserved Sequence

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

Share to Haemophilus influenzae

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Protein Domains

Share to Protein Multimerization

Source

Identifiers

PMID: 31702961
DOI: 10.1096/fj.201900681RR

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

How BamA recruits OMP substrates via poly-POTRAs domain.PMID 31702961Read ↗

The Structure of a BamA-BamD Fusion Illuminates the Architecture of the β-Barrel Assembly Machine Core.Semantic proximity Read ↗

Functioning of outer membrane protein assembly factor Omp85 requires a single POTRA domain.Semantic proximity Read ↗

Lateral opening and exit pore formation are required for BamA function.Semantic proximity Read ↗

Conserved residues of the putative L6 loop of Escherichia coli BamA play a critical role in the assembly of β-barrel outer membrane proteins, including that of BamA itself.Semantic proximity Read ↗

BamA β16C strand and periplasmic turns are critical for outer membrane protein insertion and assembly.Semantic proximity Read ↗

Outer membrane protein assembly mediated by BAM-SurA complexes.Semantic proximity Read ↗

Intrinsic flexibility of Type VII secretion central pore is required for substrate translocationSemantic proximity Read ↗

Structural control for the coordinated assembly into functional pathogenic type-3 secretion systemsSemantic proximity Read ↗

TP0326, a Treponema pallidum β‐barrel assembly machinery A (BamA) orthologue and rare outer membrane proteinSemantic proximity Read ↗

Plasticity within the barrel domain of BamA mediates a hybrid-barrel mechanism by BAM.Semantic proximity Read ↗

Structural insights into the mechanism of a novel protein targeting pathway in Gram-negative bacteria.Semantic proximity Read ↗

Structure and function of an essential component of the outer membrane protein assembly machine.Semantic proximity Read ↗

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