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Title: The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding

Journal Article · · Acta Crystallographica. Section F, Structural Biology Communications

A structure–function characterization of Synechococcus elongatus enolase (SeEN) is presented, representing the first structural report on a cyanobacterial enolase. X-ray crystal structures of SeEN in its apoenzyme form and in complex with phosphoenolpyruvate are reported at 2.05 and 2.30 Å resolution, respectively. SeEN displays the typical fold of enolases, with a conformationally flexible loop that closes the active site upon substrate binding, assisted by two metal ions that stabilize the negatively charged groups. The enzyme exhibits a catalytic efficiency of 1.2 x 105 M-1 s-1 for the dehydration of 2-phospho-D-glycerate, which is comparable to the kinetic parameters of related enzymes. These results expand the understanding of the biophysical features of these enzymes, broadening the toolbox for metabolic engineering applications.

Research Organization:
Los Alamos National Laboratory (LANL), Los Alamos, NM (United States); SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER); National Institutes of Health (NIH); Natural Sciences and Engineering Research Council of Canada (NSERC); National Research Council; Canadian Institutes of Health Research (CIHR); University of Saskatchewan; USDOE
Grant/Contract Number:
89233218CNA000001; AC02-76SF00515; P30GM133894
OSTI ID:
1862089
Alternate ID(s):
OSTI ID: 1869624
Report Number(s):
LA-UR-22-20772
Journal Information:
Acta Crystallographica. Section F, Structural Biology Communications, Vol. 78, Issue 4
Publisher:
International Union of CrystallographyCopyright Statement
Country of Publication:
United States
Language:
English