ArticleStructure (London, England : 1993)2025
Structural insights into outer membrane protein biogenesis in pathogenic Neisseria.
Evan Billings, Zixing Fan, Moloud Aflaki Sooreshjani, James C Gumbart, Nicholas Noinaj
Abstract read
In one paragraphArticle in Structure (London, England : 1993), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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5 · Who and what moneyAuthors and funding
5 authors.
Evan BillingsMarkey Center for Structural Biology, Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.
Zixing FanInterdisciplinary Bioengineering Graduate Program, Georgia Institute of Technology, Atlanta GA 30332, USA.
Moloud Aflaki SooreshjaniMarkey Center for Structural Biology, Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.
James C GumbartSchool of Physics, Georgia Institute of Technology, Atlanta GA 30332, USA; School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332, USA.
Nicholas NoinajMarkey Center for Structural Biology, Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA; Purdue Institute of Inflammation, Immunology and Infectious Disease, Purdue University, West Lafayette, IN 47907, USA. Electronic address: nnoinaj@purdue.edu.
Funding
NCCAT: National Center for CryoEM Access and Training- Supplement for Windows 10 and FFIU24GM129539 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2018 to 2023
$53.9MQuality Assurance and Quality Control Project Management: Improving Submissions and Study Conduct in the Human Subjects Research Prior Approval ProcessUL1TR002529 · NCATS · INDIANA UNIVERSITY INDIANAPOLIS · PI MOE, SHARON M, WIEHE, SARAH ELIZABETH · 2018 to 2022
$27.2MPurdue University Molecular Biophysics Training ProgramT32GM132024 · NIGMS · PURDUE UNIVERSITY · PI Angeline Marie Lyon, John Tesmer · 2019 to 2026
$2.0MElucidating the mechanisms of protein secretion across the outer membrane by bacterial autotransportersR01GM148586 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI James C. Gumbart · 2023 to 2026
$1.8MStructural Characterization of the TOC Protein Translocon MachineryR01GM127896 · NIGMS · PURDUE UNIVERSITY · PI NOINAJ, NICHOLAS · 2018 to 2022
$1.5MDynamic characterization of outer-membrane-protein biogenesis by the BAM and TAM complexesR01GM123169 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI GUMBART, JAMES C. · 2017 to 2021
$1.4MUnraveling the mechanism by which the BAM complex mediates OMP biogenesisR01GM127884 · NIGMS · PURDUE UNIVERSITY · PI NOINAJ, NICHOLAS · 2019 to 2022
$1.2MNCATS NIH HHS UL1 TR002529NIGMS NIH HHS R01 GM123169NIGMS NIH HHS R01 GM127884NIGMS NIH HHS R01 GM127896NIGMS NIH HHS R01 GM148586NIGMS NIH HHS T32 GM132024NIGMS NIH HHS U24 GM129539
6 · The paper itselfAbstract
N. gonorrhoeae (Ngo) causes the sexually transmitted infection gonorrhea with ∼106 million infections worldwide annually. Ngo infections can result in an increased risk of acquiring HIV, infertility, and blindness. To combat Ngo infections, we report the cryoelectron microscopy (cryo-EM) structure of the Ngo β-barrel assembly machinery (NgBAM), which is responsible for the biogenesis of β-barrel outer membrane proteins (OMPs). NgBAM was observed in an inward-open state; however, the polypeptide transport-associated (POTRA) domains more closely match those found in the outward-open state in E. coli β-barrel assembly machinery (BAM). The barrel seam of NgBamA consists of partial pairing of strand β1 with β16; no outward-open state of NgBAM was observed. Molecular dynamics (MD) simulations reveal unique overall dynamics and interplay between the POTRA domains of NgBamA and NgBamD. We propose that in Ngo, initial recognition occurs in the inward-open state where the last strand of the OMP partially pairs with β1 of NgBamA and must compete off β16.
Indexed as
Bacterial Outer Membrane ProteinsNeisseria gonorrhoeaeCryoelectron MicroscopyModels, MolecularMolecular Dynamics SimulationProtein DomainsBacterial Outer Membrane Proteinscryo-EMGram-negative bacteriamembrane proteinmolecular dynamicsNeisseriaprotein folding
Identifiers
PMID40902586
PMCPMC12469859
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