Flexibility in the Periplasmic Domain of BamA Is Important for Function-Reference-Cited by-同舟云学术

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Flexibility in the Periplasmic Domain of BamA Is Important for Function

Published:2017-01 Issue:1 Volume:25 Page:94-106
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Warner Lisa R.,Gatzeva-Topalova Petia Z.,Doerner Pamela A.,Pardi Arthur,Sousa Marcelo C.

Funder

NIH

National Institute of General Medical Sciences

National Science Foundation

W.M. Keck Foundation

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference58 articles.

1. Structure of BamA, an essential factor in outer membrane protein biogenesis;Albrecht;Acta Crystallogr. D Biol. Crystallogr.,2014

2. Contact-dependent growth inhibition requires the essential outer membrane protein BamA (YaeT) as the receptor and the inner membrane transport protein AcrB;Aoki;Mol. Microbiol.,2008

3. The structure of the beta-barrel assembly machinery complex;Bakelar;Science,2016

4. The structure of a BamA-BamD fusion illuminates the architecture of the beta-barrel assembly machine core;Bergal;Structure,2016

5. Experimentally exploring the conformational space sampled by domain reorientation in calmodulin;Bertini;Proc. Natl. Acad. Sci. USA,2004

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1. The patatin-like protein PlpD forms structurally dynamic homodimers in the Pseudomonas aeruginosa outer membrane;Nature Communications;2024-05-23

2. ATP‐independent assembly machinery of bacterial outer membranes: BAM complex structure and function set the stage for next‐generation therapeutics;Protein Science;2024-01-23

3. Dissecting the Organization of a β-Barrel Assembly Machinery (BAM) Complex by Neutron Reflectometry;Methods in Molecular Biology;2024

4. Similarly slow diffusion of BAM and SecYEG complexes in live E. coli cells observed with 3D spt-PALM;Biophysical Journal;2023-11

5. The patatin-like protein PlpD forms novel structurally dynamic homodimers in thePseudomonas aeruginosaouter membrane;2023-04-17

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