8WBV

The crystal structure of linear mannose with mutant H247F of the cellobiose 2-epimerase from Caldicellulosiruptor saccharolyticus

Summary for 8WBV

• Entry DOI: 10.2210/pdb8wbv/pdb
• Descriptor: Cellobiose 2-epimerase, D-mannose, beta-D-mannopyranose, ... (5 entities in total)
• Functional Keywords: cellobiose 2-epimerase, biosynthetic protein, isomerase
• Biological source: Caldicellulosiruptor saccharolyticus
• Total number of polymer chains: 1
• Total formula weight: 47045.50

Authors

Yang, R.J.,Feng, Y.H. (deposition date: 2023-09-10, release date: 2023-10-25, Last modification date: 2024-11-13)

Primary citation

Feng, Y.,Lyu, X.,Cong, Y.,Miao, T.,Fang, B.,Zhang, C.,Shen, Q.,Matthews, M.,Fisher, A.J.,Zhang, J.Z.H.,Zhang, L.,Yang, R.
A precise swaying map for how promiscuous cellobiose-2-epimerase operate bi-reaction.
Int.J.Biol.Macromol., 253:127093-127093, 2023

PubMed Abstract: Promiscuous enzymes play a crucial role in organism survival and new reaction mining. However, comprehensive mapping of the catalytic and regulatory mechanisms hasn't been well studied due to the characteristic complexity. The cellobiose 2-epimerase from Caldicellulosiruptor saccharolyticus (CsCE) with complex epimerization and isomerization was chosen to comprehensively investigate the promiscuous mechanisms. Here, the catalytic frame of ring-opening, cis-enediol mediated catalysis and ring-closing was firstly determined. To map the full view of promiscuous CE, the structure of CsCE complex with the isomerized product glucopyranosyl-β1,4-fructose was determined. Combined with computational calculation, the promiscuity was proved a precise cooperation of the double subsites, loop rearrangement, and intermediate swaying. The flexible loop was like a gear, whose structural reshaping regulates the sway of the intermediates between the two subsites of H377-H188 and H377-H247, and thus regulates the catalytic directions. The different protonated states of cis-enediol intermediate catalyzed by H188 were the key point for the catalysis. The promiscuous enzyme tends to utilize all elements at hand to carry out the promiscuous functions.

PubMed: 37758108
DOI: 10.1016/j.ijbiomac.2023.127093

Experimental method

X-RAY DIFFRACTION (1.95 Å)