5J76
Structure of Lectin from Colocasia esculenta(L.) Schott
Summary for 5J76
| Entry DOI | 10.2210/pdb5j76/pdb |
| Descriptor | 12kD storage protein, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | sugar binding, lectin, colocasia agglutinin, sugar binding protein |
| Biological source | Colocasia esculenta (Wild taro) More |
| Total number of polymer chains | 2 |
| Total formula weight | 24578.28 |
| Authors | Vajravijayan, S.,Pletnev, S.,Nandhagopal, N.,Gunasekaran, K. (deposition date: 2016-04-06, release date: 2016-06-22, Last modification date: 2024-11-06) |
| Primary citation | Vajravijayan, S.,Pletnev, S.,Pletnev, V.Z.,Nandhagopal, N.,Gunasekaran, K. Structural analysis of beta-prism lectin from Colocasia esculenta (L.) S chott. Int.J.Biol.Macromol., 91:518-523, 2016 Cited by PubMed Abstract: The Mannose-binding β-Prism Colocasia esculenta lectin (β-PCL) was purified from tubers using ion exchange chromatography. The purified β-PCL appeared as a single band of ∼12kDa on SDS-PAGE. β-PCL crystallizes in trigonal space group P3121 and diffracted to a resolution of 2.1Å. The structure was solved using Molecular replacement using Crocus vernus lectin (PDB: 3MEZ) as a model. From the final refined model to an R-factor of 16.5% and an Rfree of 20.4%, it has been observed that the biological unit consists of two β-Prism domains augmented through C-terminals swap over to form one of faces for each domain. Cα superposition of individual domains of β-PCL with individual domains of other related structures and superposition of whole protein structures were carried out. The higher RMS deviation for the superposition of whole structures suggest that β-prism domains assume different orientation in each structure. PubMed: 27262515DOI: 10.1016/j.ijbiomac.2016.05.048 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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