2FK5

Crystal structure of l-fuculose-1-phosphate aldolase from Thermus thermophilus HB8

2FK5 の概要

• エントリーDOI: 10.2210/pdb2fk5/pdb
• 関連するPDBエントリー: 2FLF
• 分子名称: fuculose-1-phosphate aldolase, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: class ii aldolase, metal binding, fuculose phosphate, riken structural genomics/proteomics initiative, rsgi, nppsfa, national project on protein structural and functional analyses, lyase
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43575.51

構造登録者

Jeyakanthan, J.,Shiro, Y.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2006-01-04, 公開日: 2007-01-04, 最終更新日: 2023-10-25)

主引用文献

Jeyakanthan, J.,Taka, J.,Kikuchi, A.,Kuroishi, C.,Yutani, K.,Shiro, Y.
Purification, crystallization and preliminary X-ray crystallographic study of the L-fuculose-1-phosphate aldolase (FucA) from Thermus thermophilus HB8
Acta Crystallogr.,Sect.F, 61:1075-1077, 2005

PubMed Abstract: Fuculose phosphate aldolase catalyzes the reversible cleavage of L-fuculose-1-phosphate to dihydroxyacetone phosphate and L-lactaldehyde. The protein from Thermus thermophilus HB8 is a biological tetramer with a subunit molecular weight of 21 591 Da. Purified FucA has been crystallized using sitting-drop vapour-diffusion and microbatch techniques at 293 K. The crystals belong to space group P4, with unit-cell parameters a = b = 100.94, c = 45.87 A. The presence of a dimer of the enzyme in the asymmetric unit was estimated to give a Matthews coefficient (VM) of 2.7 A3 Da(-1) and a solvent content of 54.2%(v/v). Three-wavelength diffraction MAD data were collected to 2.3 A from zinc-containing crystals. Native diffraction data to 1.9 A resolution have been collected using synchrotron radiation at SPring-8.

PubMed: 16511238
DOI: 10.1107/S1744309105036766

実験手法

X-RAY DIFFRACTION (1.9 Å)