3U4X

Crystal structure of a lectin from Camptosema pedicellatum seeds in complex with 5-bromo-4-chloro-3-indolyl-alpha-D-mannose

Summary for 3U4X

• Entry DOI: 10.2210/pdb3u4x/pdb
• Descriptor: Camptosema pedicellatum lectin (CPL), CALCIUM ION, MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: jelly-roll domain, lectin, carbohydrate-binding protein
• Biological source: Camptosema pedicellatum
• Total number of polymer chains: 1
• Total formula weight: 25823.50

Authors

Rocha, B.A.M.,Teixeira, C.S.,Moura, T.R.,Silva, H.C.,Pereira-Junior, F.N.,Nagano, C.S.,Delatorre, P.,Cavada, B.S. (deposition date: 2011-10-10, release date: 2012-09-12, Last modification date: 2024-02-28)

Primary citation

Souza Teixeira, C.,Colares da Silva, H.,Rocha de Moura, T.,Pereira-Junior, F.N.,Santiago do Nascimento, K.,Shiniti Nagano, C.,Holanda Sampaio, A.,Delatorre, P.,Matias Rocha, B.A.,Sousa Cavada, B.
Crystal structure of the lectin of Camptosema pedicellatum: implications of a conservative substitution at the hydrophobic subsite.
J.Biochem., 152:87-98, 2012

PubMed Abstract: Lectins have been used as models for studies of the molecular basis of protein-carbohydrate interaction and specificity by deciphering codes present in the glycan structures. The purpose of the present study was to purify and solve the complete primary and crystal structure of the lectin of Camptosema pedicellatum (CPL) complexed with 5-bromo-4-chloro-3-indolyl-α-d-mannose (X-Man) using tandem mass spectrometry. CPL was purified by single-step affinity chromatography. Mass spectrometry findings revealed that purified CPL features a combination of chains weighing 25,298 ± 2 (α-chain), 12,835 ± 2 (β-chain) and 12,481 ± 2 Da (γ-chain). The solved crystal structure of CPL features a conservative mutation in the hydrophobic subsite, a constituent of the carbohydrate recognition domain (CRD), indicating the relevance of hydrophobic interactions in the establishment of interactions with carbohydrates. The substitution and the analysis of the interactions with X-Man also revealed that the hydrophobic effect caused by a minor change in the hydrophobic subsite interferes in the formation of H-bonds due to the reorientation of the indolyl group in the CRD.

PubMed: 22554687
DOI: 10.1093/jb/mvs047

Experimental method

X-RAY DIFFRACTION (2.16 Å)