1AY2

STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Work: 0.194 
  • R-Value Observed: 0.194 

wwPDB Validation   3D Report Full Report


This is version 3.0 of the entry. See complete history


Literature

Structure of the fibre-forming protein pilin at 2.6 A resolution.

Parge, H.E.Forest, K.T.Hickey, M.J.Christensen, D.A.Getzoff, E.D.Tainer, J.A.

(1995) Nature 378: 32-38

  • DOI: https://doi.org/10.1038/378032a0
  • Primary Citation of Related Structures:  
    1AY2

  • PubMed Abstract: 

    The crystallographic structure of Neisseria gonorrhoeae pilin, which assembles into the multifunctional pilus adhesion and virulence factor, reveals an alpha-beta roll fold with a striking 85 A alpha-helical spine and an O-linked disaccharide. Key residues stabilize interactions that allow sequence hypervariability, responsible for pilin's celebrated antigenic variation, within disulphide region beta-strands and connections. Pilin surface shape, hydrophobicity and sequence variation constrain pilus assembly to the packing of flat subunit faces against alpha 1 helices. Helical fibre assembly is postulated to form a core of coiled alpha 1 helices banded by beta-sheet, leaving carbohydrate and hypervariable sequence regions exposed to solvent.


  • Organizational Affiliation

    Department of Molecular Biology, Scripps Research Institute, La Jolla, California 92037, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TYPE 4 PILIN158Neisseria gonorrhoeaeMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for P02974 (Neisseria gonorrhoeae)
Explore P02974 
Go to UniProtKB:  P02974
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP02974
Sequence Annotations
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  • Reference Sequence
Oligosaccharides

Help

Entity ID: 2
MoleculeChains Length2D Diagram Glycosylation3D Interactions
alpha-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose
B
2O-Glycosylation
Glycosylation Resources
GlyTouCan:  G15031WB
GlyCosmos:  G15031WB
GlyGen:  G15031WB
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Work: 0.194 
  • R-Value Observed: 0.194 
  • Space Group: C 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 127.58α = 90
b = 121.08β = 90
c = 26.86γ = 90
Software Package:
Software NamePurpose
MOSFLMdata reduction
ROTAVATAdata reduction
Agrovatadata reduction
X-PLORmodel building
X-PLORrefinement
CCP4data scaling
ROTAVATAdata scaling
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-04-29
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Non-polymer description, Version format compliance
  • Version 2.0: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Atomic model, Data collection, Derived calculations, Refinement description, Structure summary
  • Version 3.0: 2023-02-15
    Changes: Advisory, Atomic model, Data collection, Database references, Derived calculations, Non-polymer description, Polymer sequence, Structure summary