2DSU

Binding of chitin-like polysaccharide to protective signalling factor: Crystal structure of the complex formed between signalling protein from sheep (SPS-40) with a tetrasaccharide at 2.2 A resolution


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.209 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.187 

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This is version 2.1 of the entry. See complete history


Literature

Carbohydrate binding properties and carbohydrate induced conformational switch in sheep secretory glycoprotein (SPS-40): crystal structures of four complexes of SPS-40 with chitin-like oligosaccharides

Srivastava, D.B.Ethayathulla, A.S.Kumar, J.Somvanshi, R.K.Sharma, S.Dey, S.Singh, T.P.

(2007) J Struct Biol 158: 255-266

  • DOI: https://doi.org/10.1016/j.jsb.2006.11.002
  • Primary Citation of Related Structures:  
    2DSU, 2DSV, 2DSW, 2G41

  • PubMed Abstract: 

    Crystal structures of four complexes of sheep secretory glycoprotein (SPS-40) with N-acetylglucosamine oligosaccharides (GlcNAc(n), (n=3-6)) have been determined at moderate resolutions. The binding studies of SPS-40 have been carried out using fluorescence spectroscopy and Surface Plasmon Resonance (SPR). Structure determinations of four complexes have shown a novel binding pattern of GlcNAc(n) molecules to SPS-40. The results indicate that the most preferred recognition region in the carbohydrate binding groove in SPS-40 is at subsites -4 to -2 among which subsite -2 provides the maximum interactions with carbohydrate residues. These structures have also shown that the interactions of GlcNAc3 and GlcNAc4 do not perturb the protein structure and those of GlcNAc5 induce partial conformational changes while in the case of GlcNAc6 the partially closed binding groove opened up completely. As in other SPX-40 structures, SPS-40 structure contains three overlapping flexible surface segments, His188-His197, Phe202-Arg212 and Phe244-Pro260 with several charged residues protruding outwardly. It creates a cluster of positive charges with a flexible base thus indicating a good scope of promoting the intermolecular interactions. This protein is glycosylated at Asn39 and may recognize other receptors having sugar binding sites. It appears that SPS-40 may involve both carbohydrate and protein bindings. The systematic carbohydrate-binding studies and the detailed structural results of four protein-carbohydrate complexes provide an excellent insight into the mechanism of carbohydrate binding. These are the first studies of this kind on secretory glycoproteins and their interactions with carbohydrates.


  • Organizational Affiliation

    Department of Biophysics, All India Institute of Medical Sciences, New Delhi 110029, India.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Chitinase-3-like protein 1361Ovis ariesMutation(s): 0 
UniProt
Find proteins for Q6TMG6 (Ovis aries)
Explore Q6TMG6 
Go to UniProtKB:  Q6TMG6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6TMG6
Sequence Annotations
Expand
  • Reference Sequence
Oligosaccharides

Help

Entity ID: 2
MoleculeChains Length2D Diagram Glycosylation3D Interactions
alpha-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
B
4N-Glycosylation
Glycosylation Resources
GlyTouCan:  G23782GU
GlyCosmos:  G23782GU
GlyGen:  G23782GU
Entity ID: 3
MoleculeChains Length2D Diagram Glycosylation3D Interactions
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose
C
4N/A
Glycosylation Resources
GlyTouCan:  G93613RO
GlyCosmos:  G93613RO
GlyGen:  G93613RO
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.209 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.187 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 62.75α = 90
b = 66.51β = 90
c = 107.574γ = 90
Software Package:
Software NamePurpose
CNSrefinement
AUTOMARdata reduction
SCALEPACKdata scaling
AMoREphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-07-25
    Type: Initial release
  • Version 1.1: 2008-04-30
    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, Structure summary
  • Version 2.1: 2023-10-25
    Changes: Data collection, Database references, Refinement description, Structure summary