8UEL

Crystal structure of enolase from Litopenaeus vannamei

Summary for 8UEL

• Entry DOI: 10.2210/pdb8uel/pdb
• Descriptor: Enolase, PHOSPHOENOLPYRUVATE, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: lyase, litopenaeus vannamei, metal protein
• Biological source: Penaeus vannamei
• Total number of polymer chains: 2
• Total formula weight: 95120.79

Authors

Chang, X.,Zhao, G. (deposition date: 2023-10-01, release date: 2023-12-13, Last modification date: 2024-11-20)

Primary citation

Chang, X.,Zhang, T.,Zang, J.,Lv, C.,Zhao, G.
Characterization and Structural Analyses of Enolase from Shrimp ( Litopenaeus vannamei ).
J.Agric.Food Chem., 71:19783-19790, 2023

PubMed Abstract: Transcriptome analysis had recognized enolase from shrimp (), which is termed LvEnolase, as one of the allergens, but its amino acid sequence and protein structure have been lacking. In this study, natural LvEnolase was isolated from and characterized for the first time. The full-length cDNA sequence of LvEnolase was effectively cloned, which encoded 434 amino acid residues. The crystal structure of LvEnolase was successfully determined at a resolution of 2.5 Å by X-ray crystallography (PDB: 8UEL). Notably, it was observed that near the active center, a loop exists in either an open or closed state, and the open loop was associated with the product release phase. Furthermore, enzyme activity assays were conducted to validate the catalytic capabilities of purified LvEnolase. These findings significantly enhance our comprehension of the enolase family and provide valuable support for delving into the functions and characteristics of LvEnolase.

PubMed: 38033172
DOI: 10.1021/acs.jafc.3c07135

Experimental method

X-RAY DIFFRACTION (2.49 Å)