1MZO

Crystal structure of pyruvate formate-lyase with pyruvate

Summary for 1MZO

• Entry DOI: 10.2210/pdb1mzo/pdb
• Descriptor: Pyruvate formate-lyase, TRIETHYLENE GLYCOL, PYRUVIC ACID, ... (4 entities in total)
• Functional Keywords: enzyme-substrate complex, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P09373
• Total number of polymer chains: 2
• Total formula weight: 170982.09

Authors

Lehtio, L.,Leppanen, V.-M.,Kozarich, J.W.,Goldman, A. (deposition date: 2002-10-09, release date: 2002-12-11, Last modification date: 2023-11-15)

Primary citation

Lehtio, L.,Leppanen, V.M.,Kozarich, J.W.,Goldman, A.
Structure of Escherichia coli pyruvate formate-lyase with pyruvate.
Acta Crystallogr.,Sect.D, 58:2209-2212, 2002

PubMed Abstract: The structure of inactive pyruvate formate-lyase in complex with a natural substrate, pyruvate, was solved at 2.7 A resolution. Both active sites of the homodimeric enzyme are occupied by pyruvate; additional binding sites were not found. Pyruvate was found in a cleft close to the active-site cysteines 418 and 419, with the carboxyl group in contact with arginines 176 and 435 and the methyl group within van der Waals distance of Phe327. It is believed that the binding site of pyruvate is not the position of pyruvate as the reaction initiates, as conformational changes occur during activation of the enzyme.

PubMed: 12454503
DOI: 10.1107/S0907444902016402

Experimental method

X-RAY DIFFRACTION (2.7 Å)