1T0W

25 NMR structures of Truncated Hevein of 32 aa (Hevein-32) complex with N,N,N-triacetylglucosamina

Summary for 1T0W

• Entry DOI: 10.2210/pdb1t0w/pdb
• Related: 1HEV 1MMC 1Q9B
• NMR Information: BMRB: 6123
• Related PRD ID: PRD_900017
• Descriptor: Hevein, 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 (2 entities in total)
• Functional Keywords: alpha-helix, anti-parallel beta-sheet, sugar binding protein
• Total number of polymer chains: 1
• Total formula weight: 4112.45

Authors

Aboitiz, N.,Vila-Perello, M.,Groves, P.,Asensio, J.L.,Andreu, D.,Canada, F.J.,Jimenez-Barbero, J. (deposition date: 2004-04-13, release date: 2004-09-28, Last modification date: 2024-10-30)

Primary citation

Aboitiz, N.,Vila-Perello, M.,Groves, P.,Asensio, J.L.,Andreu, D.,Canada, F.J.,Jimenez-Barbero, J.
NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides
Chembiochem, 5:1245-1245, 2004

PubMed Abstract: HEV32, a 32-residue, truncated hevein lacking eleven C-terminal amino acids, was synthesized by solid-phase methodology and correctly folded with three cysteine bridge pairs. The affinities of HEV32 for small chitin fragments--in the forms of N,N',N"-triacetylchitotriose ((GlcNAc)3) (millimolar) and N,N',N",N"',N"",N""'-hexaacetylchitohexaose ((GlcNAc)6) (micromolar)--as measured by NMR and fluorescence methods, are comparable with those of native hevein. The HEV32 ligand-binding process is enthalpy driven, while entropy opposes binding. The NMR structure of ligand-bound HEV32 in aqueous solution was determined to be highly similar to the NMR structure of ligand-bound hevein. Solvated molecular-dynamics simulations were performed in order to monitor the changes in side-chain conformation of the binding site of HEV32 and hevein upon interaction with ligands. The calculations suggest that the Trp21 side-chain orientation of HEV32 in the free form differs from that in the bound state; this agrees with fluorescence and thermodynamic data. HEV32 provides a simple molecular model for studying protein-carbohydrate interactions and for understanding the physiological relevance of small native hevein domains lacking C-terminal residues.

PubMed: 15368576
DOI: 10.1002/cbic.200400025

Experimental method

SOLUTION NMR