7WBO

Crystal structure of Sarcoplasmic Calcium-Binding Protein from Scylla paramamosain

Summary for 7WBO

• Entry DOI: 10.2210/pdb7wbo/pdb
• Descriptor: Sarcoplasmic calcium-binding protein, 1,2-ETHANEDIOL, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: allergy, scylla paramamosain, ef-hand, allergen
• Biological source: Scylla paramamosain (green mud crab)
• Total number of polymer chains: 1
• Total formula weight: 22977.83

Authors

Chen, Y.,Jin, T.,Liu, G. (deposition date: 2021-12-17, release date: 2022-12-21, Last modification date: 2023-11-29)

Primary citation

Chen, Y.,Jin, T.,Li, M.,Yun, X.,Huan, F.,Liu, Q.,Hu, M.,Wei, X.,Zheng, P.,Liu, G.
Crystal Structure Analysis of Sarcoplasmic-Calcium-Binding Protein: An Allergen in Scylla paramamosain.
J.Agric.Food Chem., 71:1214-1223, 2023

PubMed Abstract: The structure of allergenic proteins provides important information about the binding of allergens to antibodies. In this study, the crystal structure of Scy p 4 with a resolution of 1.60 Å was obtained by X-ray diffraction. Epitope mapping of Scy p 4 revealed that linear epitopes are located on the surface of Scy p 4. Also, conformational epitopes are mostly located in the structural conservative region. Further structural comparison, surface electrostatic potential, and hydrogen bond force analysis showed that mutation of Asp and Asp would lead to calcium-binding capacity being lost and destruction of allergenicity. Furthermore, a comparative analysis of structure showed that sarcoplasmic-calcium-binding protein (SCP) had high sequence, secondary, and spatial structural identity in crustaceans, which may be an important factor leading to cross-reactivity among crustaceans. The structure of Scy p 4 provides a template for epitope evaluation and localization of SCPs, which will help to reveal cross-reactivity among species.

PubMed: 36602420
DOI: 10.1021/acs.jafc.2c07267

Experimental method

X-RAY DIFFRACTION (1.6 Å)