3SNM

Crystal structure of a lectin from Canavalia maritima seeds complexed with Indole-3-Acetic Acid


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.15 Å
  • R-Value Free: 0.225 
  • R-Value Work: 0.206 
  • R-Value Observed: 0.207 

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This is version 1.2 of the entry. See complete history


Literature

Interactions between indole-3-acetic acid (IAA) with a lectin from Canavalia maritima seeds reveal a new function for lectins in plant physiology.

Delatorre, P.Silva-Filho, J.C.Rocha, B.A.Santi-Gadelha, T.da Nobrega, R.B.Gadelha, C.A.do Nascimento, K.S.Nagano, C.S.Sampaio, A.H.Cavada, B.S.

(2013) Biochimie 95: 1697-1703

  • DOI: https://doi.org/10.1016/j.biochi.2013.05.008
  • Primary Citation of Related Structures:  
    3SNM

  • PubMed Abstract: 

    Indole-3-acetic acid (IAA) bound is considered a storage molecule and is inactive. However, some studies have proposed an additional possible regulatory mechanism based on the ability of lectins to form complexes with IAA. We report the first crystal structure of ConM in complex with IAA at 2.15 Å resolution. Based on a tetrameric model of the complex, we hypothesize how the lectin controls the availability of IAA during the early seedling stages, indicating a possible new physiological role for these proteins. A free indole group is also bound to the protein. The ConM interaction with different forms of IAA is a strategy to render the phytohormone unavailable to the cell. Thus, this new physiological role proposed for legume lectins might be a novel mechanism by which IAA levels are decreased in addition to the destruction and formation of new complexes in the later stages of seed germination.


  • Organizational Affiliation

    Departamento de Biologia Molecular, Universidade Federal da Paraíba, João Pessoa, Brazil. [email protected]


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Concanavalin-A237Canavalia lineataMutation(s): 0 
UniProt
Find proteins for P81460 (Canavalia lineata)
Explore P81460 
Go to UniProtKB:  P81460
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP81460
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.15 Å
  • R-Value Free: 0.225 
  • R-Value Work: 0.206 
  • R-Value Observed: 0.207 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 67.19α = 90
b = 70.74β = 90
c = 97.75γ = 90
Software Package:
Software NamePurpose
iMOSFLMdata reduction
Cootmodel building
REFMACrefinement
SCALAdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-08-01
    Type: Initial release
  • Version 1.1: 2013-08-21
    Changes: Database references
  • Version 1.2: 2024-02-28
    Changes: Data collection, Database references, Derived calculations