3GZH

Crystal structure of phosphate-bound adenylosuccinate lyase from E. coli

Summary for 3GZH

• Entry DOI: 10.2210/pdb3gzh/pdb
• Descriptor: Adenylosuccinate lyase, SODIUM ION, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: all-helical fold, adenylosuccinate lyase, structural genomics, bacterial structural genomics initiative, montreal-kingston bacterial structural genomics initiative, bsgi, lyase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 54951.75

Authors

Kozlov, G.,Gehring, K.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2009-04-07, release date: 2009-08-25, Last modification date: 2023-09-06)

Primary citation

Kozlov, G.,Nguyen, L.,Pearsall, J.,Gehring, K.
The structure of phosphate-bound Escherichia coli adenylosuccinate lyase identifies His171 as a catalytic acid.
Acta Crystallogr.,Sect.F, 65:857-861, 2009

PubMed Abstract: Adenylosuccinate lyase (ASL) is an enzyme from the purine-biosynthetic pathway that catalyzes the cleavage of 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) to 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) and fumarate. ASL is also responsible for the conversion of succinyladenosine monophosphate (SAMP) to adenosine monophosphate (AMP) and fumarate. Here, the crystal structure of adenylosuccinate lyase from Escherichia coli was determined to 1.9 A resolution. The enzyme adopts a substrate-bound conformation as a result of the presence of two phosphate ions bound in the active site. Comparison with previously solved structures of the apoenzyme and an SAMP-bound H171A mutant reveals a conformational change at His171 associated with substrate binding and confirms the role of this residue as a catalytic acid.

PubMed: 19724117
DOI: 10.1107/S1744309109029674

Experimental method

X-RAY DIFFRACTION (1.9 Å)