3GZH

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

3GZH の概要

• エントリーDOI: 10.2210/pdb3gzh/pdb
• 分子名称: Adenylosuccinate lyase, SODIUM ION, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: all-helical fold, adenylosuccinate lyase, structural genomics, bacterial structural genomics initiative, montreal-kingston bacterial structural genomics initiative, bsgi, lyase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54951.75

構造登録者

Kozlov, G.,Gehring, K.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (登録日: 2009-04-07, 公開日: 2009-08-25, 最終更新日: 2023-09-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)