4G13

Crystal structure of samarosporin I at 100K


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 0.80 Å
  • R-Value Free: 0.081 
  • R-Value Work: 0.078 
  • R-Value Observed: 0.078 

wwPDB Validation 3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The crystal structure of samarosporin I at atomic resolution.

Gessmann, R.Axford, D.Evans, G.Bruckner, H.Petratos, K.

(2012) J Pept Sci 18: 678-684

  • DOI: 10.1002/psc.2454
  • Structures With Same Primary Citation

  • PubMed Abstract: 
  • The atomic resolution structures of samarosporin I have been determined at 100 and 293 K. This is the first crystal structure of a natural 15-residue peptaibol. The amino acid sequence in samarosporin I is identical to emerimicin IV and stilbellin I. ...

    The atomic resolution structures of samarosporin I have been determined at 100 and 293 K. This is the first crystal structure of a natural 15-residue peptaibol. The amino acid sequence in samarosporin I is identical to emerimicin IV and stilbellin I. Samarosporin is a peptide antibiotic produced by the ascomycetous fungus Samarospora rostrup and belongs to peptaibol subfamily 2. The structures at both temperatures are very similar to each other adopting mainly a 3₁₀-helical and a minor fraction of α-helical conformation. The helices are significantly bent and packed in an antiparallel fashion in the centered monoclinic lattice leaving among them an approximately 10-Å channel extending along the crystallographic twofold axis. Only two ordered water molecules per peptide molecule were located in the channel. Comparisons have been carried out with crystal structures of subfamily 2 16-residue peptaibols antiamoebin and cephaibols. The repercussion of the structural analysis of samarosporin on membrane function is discussed.


    Organizational Affiliation

    IMBB-FORTH, N. Plastira 100, Heraklion 70013, Greece.



Macromolecules
  • Find similar proteins by: Sequence   |   Structure
Entity ID: 1
MoleculeChainsSequence LengthOrganismDetails
SAMAROSPORIN I
A
16N/AMutation(s): 0 
Protein Feature View is not available: No corresponding UniProt sequence found.
Small Molecules
Biologically Interesting Molecules 1 Unique
IDChainsNameType/Class2D Diagram3D Interactions
PRD_000920
Query on PRD_000920
ASAMAROSPORIN IPeptaibol /  Antibiotic

--

Modified Residues  3 Unique
IDChainsTypeFormula2D DiagramParent
AIB
Query on AIB
A
L-PEPTIDE LINKINGC4 H9 N O2ALA
HYP
Query on HYP
A
L-PEPTIDE LINKINGC5 H9 N O3PRO
PHL
Query on PHL
A
L-PEPTIDE LINKINGC9 H13 N OPHE
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 0.80 Å
  • R-Value Free: 0.081 
  • R-Value Work: 0.078 
  • R-Value Observed: 0.078 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 45.109α = 90
b = 9.075β = 115.6
c = 25.067γ = 90
Software Package:
Software NamePurpose
ACORNphasing
SHELXL-97refinement
XDSdata reduction
SCALAdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History 

  • Version 1.0: 2012-10-03
    Type: Initial release
  • Version 1.1: 2012-10-31
    Changes: Database references
  • Version 1.2: 2012-12-26
    Changes: Database references, Structure summary
  • Version 1.3: 2018-07-18
    Changes: Data collection, Database references