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PDBsum entry 2dvb

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protein ligands metals Protein-protein interface(s) links
Sugar binding protein PDB id
2dvb

 

 

 

 

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Contents
Protein chains
232 a.a. *
Ligands
NGA-GAL
SO4 ×4
GAL ×3
Metals
_CA ×4
_MN ×4
Waters ×985
* Residue conservation analysis
PDB id:
2dvb
Name: Sugar binding protein
Title: Crystal structure of peanut lectin gal-beta-1,6-galnac complex
Structure: Galactose-binding lectin. Chain: a, b, c, d. Fragment: residues 1-236. Synonym: agglutinin, pna
Source: Arachis hypogaea. Peanut. Organism_taxid: 3818
Biol. unit: Tetramer (from PQS)
Resolution:
2.25Å     R-factor:   0.214     R-free:   0.266
Authors: S.K.Natchiar,O.Srinivas,N.Mitra,A.Surolia,N.Jayaraman,M.Vijayan
Key ref:
S.K.Natchiar et al. (2006). Structural studies on peanut lectin complexed with disaccharides involving different linkages: further insights into the structure and interactions of the lectin. Acta Crystallogr D Biol Crystallogr, 62, 1413-1421. PubMed id: 17057347 DOI: 10.1107/S0907444906035712
Date:
30-Jul-06     Release date:   07-Nov-06    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P02872  (LECG_ARAHY) -  Galactose-binding lectin from Arachis hypogaea
Seq:
Struc:
273 a.a.
232 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1107/S0907444906035712 Acta Crystallogr D Biol Crystallogr 62:1413-1421 (2006)
PubMed id: 17057347  
 
 
Structural studies on peanut lectin complexed with disaccharides involving different linkages: further insights into the structure and interactions of the lectin.
S.K.Natchiar, O.Srinivas, N.Mitra, A.Surolia, N.Jayaraman, M.Vijayan.
 
  ABSTRACT  
 
Crystal structures of peanut lectin complexed with Galbeta1-3Gal, methyl-T-antigen, Galbeta1-6GalNAc, Galalpha1-3Gal and Galalpha1-6Glc and that of a crystal grown in the presence of Galalpha1-3Galbeta1-4Gal have been determined using data collected at 100 K. The use of water bridges as a strategy for generating carbohydrate specificity was previously deduced from the complexes of the lectin with lactose (Galbeta1-4Glc) and T-antigen (Galbeta1-3GalNAc). This has been confirmed by the analysis of the complexes with Galbeta1-3Gal and methyl-T-antigen (Galbeta1-3GalNAc-alpha-OMe). A detailed analysis of lectin-sugar interactions in the complexes shows that they are more extensive when the beta-anomer is involved in the linkage. As expected, the second sugar residue is ill-defined when the linkage is 1-->6. There are more than two dozen water molecules which occur in the hydration shells of all structures determined at resolutions better than 2.5 A. Most of them are involved in stabilizing the structure, particularly loops. Water molecules involved in lectin-sugar interactions are also substantially conserved. The lectin molecule is fairly rigid and does not appear to be affected by changes in temperature.
 
  Selected figure(s)  
 
Figure 2.
Figure 2 A PNA monomer with invariant water molecules and the two metal ions. See text for details.
Figure 6.
Figure 6 Stereoview of water bridges involving invariant water molecules in the metal- and sugar-binding region.
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2006, 62, 1413-1421) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20729346 A.Sharma, and M.Vijayan (2011).
Influence of glycosidic linkage on the nature of carbohydrate binding in beta-prism I fold lectins: an X-ray and molecular dynamics investigation on banana lectin-carbohydrate complexes.
  Glycobiology, 21, 23-33.
PDB codes: 3mit 3miu 3miv
19496993 G.Pandey, T.Fatma, and S.S.Komath (2009).
Specific interaction of the legume lectins, concanavalin a and peanut agglutinin, with phycocyanin.
  Photochem Photobiol, 85, 1126-1133.  
18227943 C.Gondran, M.P.Dubois, S.Fort, S.Cosnier, and S.Szunerits (2008).
Detection of carbohydrate-binding proteins by oligosaccharide-modified polypyrrole interfaces using electrochemical surface plasmon resonance.
  Analyst, 133, 206-212.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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