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- PDB-9lab: Cryo-EM structure of Shewanella oneidensis MR-1 MshA pili. -

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Basic information

Entry
Database: PDB / ID: 9lab
TitleCryo-EM structure of Shewanella oneidensis MR-1 MshA pili.
ComponentsMSHA major pilin subunit MshA
KeywordsCELL ADHESION / MSHA major pilin subunit MshA
Function / homologyProkaryotic N-terminal methylation site. / Prokaryotic N-terminal methylation motif / Prokaryotic N-terminal methylation site / Pilin-like / membrane / MSHA major pilin subunit MshA
Function and homology information
Biological speciesShewanella oneidensis MR-1 (bacteria)
MethodELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.6 Å
AuthorsLi, D.N. / Liu, C.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: To Be Published
Title: MSHA major pilin subunit MshA
Authors: Li, D.N. / Liu, C.
History
DepositionJan 2, 2025Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Jan 7, 2026Provider: repository / Type: Initial release
Revision 1.0Jan 7, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Jan 7, 2026Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0Jan 7, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jan 7, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jan 7, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Jan 7, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
B: MSHA major pilin subunit MshA
C: MSHA major pilin subunit MshA
D: MSHA major pilin subunit MshA
E: MSHA major pilin subunit MshA
F: MSHA major pilin subunit MshA
G: MSHA major pilin subunit MshA
H: MSHA major pilin subunit MshA
I: MSHA major pilin subunit MshA


Theoretical massNumber of molelcules
Total (without water)141,3618
Polymers141,3618
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein
MSHA major pilin subunit MshA


Mass: 17670.186 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) Shewanella oneidensis MR-1 (bacteria) / References: UniProt: Q8EA04
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: FILAMENT / 3D reconstruction method: helical reconstruction

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Sample preparation

ComponentName: Cryo-EM structure of Shewanella oneidensis MR-1 MshA pili.
Type: CELL / Entity ID: all / Source: NATURAL
Molecular weightExperimental value: NO
Source (natural)Organism: Shewanella oneidensis MR-1 (bacteria)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 7
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

MicroscopyModel: FEI TECNAI 12
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 55 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

CTF correctionType: NONE
Helical symmertyAngular rotation/subunit: 81.06 ° / Axial rise/subunit: 11.92 Å / Axial symmetry: C1
3D reconstructionResolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 15544 / Symmetry type: HELICAL
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0069144
ELECTRON MICROSCOPYf_angle_d0.56512432
ELECTRON MICROSCOPYf_dihedral_angle_d8.1375448
ELECTRON MICROSCOPYf_chiral_restr0.0381528
ELECTRON MICROSCOPYf_plane_restr0.0031560

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