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- PDB-9nz5: MERSmut-CoV M protein dimer in complex with FAb B -

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Basic information

Entry
Database: PDB / ID: 9nz5
TitleMERSmut-CoV M protein dimer in complex with FAb B
Components
  • FAb B heavy chain
  • FAb B light chain
  • Membrane protein
KeywordsMEMBRANE PROTEIN/IMMUNE SYSTEM/INHIBITOR / M protein / SARS-CoV-2 / inhibitor bound complex / viral protein / MEMBRANE PROTEIN-IMMUNE SYSTEM-INHIBITOR complex
Function / homology
Function and homology information


host cell Golgi membrane / structural constituent of virion / viral envelope / virion membrane / membrane
Similarity search - Function
M matrix/glycoprotein, MERS-like-CoV / M matrix/glycoprotein, coronavirus / Coronavirus M matrix/glycoprotein / Coronavirus membrane (Cov-M) protein profile.
Similarity search - Domain/homology
Biological speciesMiddle East respiratory syndrome-related coronavirus
Homo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.15 Å
AuthorsMann, M.K. / Abeywickrema, P.
Funding support United States, 1items
OrganizationGrant numberCountry
Department of Health & Human Services (HHS)HHSO100201700018C United States
CitationJournal: Commun Biol / Year: 2025
Title: Structural insights into MERS and SARS coronavirus membrane proteins.
Authors: Mandeep Kaur Mann / Yanting Yin / Simone Marsili / Jiexiong Xie / Jordi Doijen / Robyn Miller / Madison Piassek / Nick van den Broeck / Christopher Kinyanjui Kariuki / Heidi L M de Gruyter / ...Authors: Mandeep Kaur Mann / Yanting Yin / Simone Marsili / Jiexiong Xie / Jordi Doijen / Robyn Miller / Madison Piassek / Nick van den Broeck / Christopher Kinyanjui Kariuki / Heidi L M de Gruyter / Anouk A Leijs / Eric J Snijder / Martijn J van Hemert / Ken Keustermans / Michiel Van Gool / Xiaodi Yu / Marnix van Loock / Anil Koul / Sujata Sharma / Ellen Van Damme / Pravien Abeywickrema /
Abstract: The membrane (M) protein of coronaviruses is essential for maintaining structural integrity during membrane virion budding and viral pathogenesis. Given its high conservation in lineages within the ...The membrane (M) protein of coronaviruses is essential for maintaining structural integrity during membrane virion budding and viral pathogenesis. Given its high conservation in lineages within the betacoronavirus genus, such as sarbecoviruses, the M protein presents as an attractive therapeutic target; however, developing broad-spectrum antivirals targeting coronaviruses such as MERS-CoV is challenging due to lower sequence conservation and limited structural information available beyond that of the SARS-CoV-2 M protein. In this study, we report 3-3.2 Å resolution structures of MERS-CoV M protein, engineered with a SARS-CoV-2-like antibody interface, representing the first human merbecovirus M protein structure, and SARS-CoV M protein structures, with and without a previously identified SARS-CoV-2 M protein inhibitor, JNJ-9676. We highlight the structural differences between the MERS-CoV, SARS-CoV and SARS-CoV-2 M proteins, and present insights into the conservation of the JNJ-9676 binding pocket as well as key differences that could be targeted to accelerate the design of specific MERS-CoV and broad-spectrum antivirals targeting coronavirus M proteins.
History
DepositionMar 31, 2025Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 29, 2025Provider: repository / Type: Initial release
Revision 1.0Oct 29, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Oct 29, 2025Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Oct 29, 2025Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Oct 29, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Oct 29, 2025Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release
Revision 1.1Dec 3, 2025Group: Data collection / Database references / Category: citation / citation_author / em_admin
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.pdbx_database_id_DOI / _citation.title / _citation.year / _em_admin.last_update
Revision 1.2Dec 10, 2025Group: Data collection / Database references / Category: citation / em_admin
Item: _citation.page_last / _citation.pdbx_database_id_PubMed ..._citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _em_admin.last_update

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Membrane protein
D: Membrane protein
C: FAb B light chain
B: FAb B heavy chain
E: FAb B light chain
F: FAb B heavy chain


Theoretical massNumber of molelcules
Total (without water)155,8216
Polymers155,8216
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Membrane protein / M protein / E1 glycoprotein / Matrix glycoprotein / Membrane glycoprotein


Mass: 29542.191 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Middle East respiratory syndrome-related coronavirus
Gene: M, E, AL079_478421_M
Production host: Mammalian expression vector Flag-MCS-pcDNA3.1 (others)
References: UniProt: R9UNX5
#2: Antibody FAb B light chain


Mass: 24157.424 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Production host: Mammalian expression vector Flag-MCS-pcDNA3.1 (others)
#3: Antibody FAb B heavy chain


Mass: 24211.092 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Production host: Mammalian expression vector Flag-MCS-pcDNA3.1 (others)
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: MERSmut-CoV M protein dimer in complex with FAb B / Type: COMPLEX / Entity ID: all / Source: MULTIPLE SOURCES
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 7.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: NITROGEN

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: DIFFRACTION / Nominal defocus max: 2300 nm / Nominal defocus min: 1400 nm
Image recordingElectron dose: 51.96 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM software
IDNameVersionCategory
1cryoSPARCparticle selection
2PHENIX1.20.1_4487model refinement
13cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.15 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 827876 / Symmetry type: POINT
RefinementHighest resolution: 3.15 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0049940
ELECTRON MICROSCOPYf_angle_d0.83913565
ELECTRON MICROSCOPYf_dihedral_angle_d4.881356
ELECTRON MICROSCOPYf_chiral_restr0.0511541
ELECTRON MICROSCOPYf_plane_restr0.0081704

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