2FUA

L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T WITH COBALT

2FUA の概要

• エントリーDOI: 10.2210/pdb2fua/pdb
• 分子名称: L-FUCULOSE-1-PHOSPHATE ALDOLASE, COBALT (II) ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: class ii aldolase, lyase (aldehyde)
• 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: 24134.51

構造登録者

Dreyer, M.K.,Schulz, G.E. (登録日: 1996-02-14, 公開日: 1996-10-14, 最終更新日: 2024-06-05)

主引用文献

Dreyer, M.K.,Schulz, G.E.
Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli.
Acta Crystallogr.,Sect.D, 52:1082-1091, 1996

PubMed Abstract: The structure of the class II zinc-ion dependent L-fuculose-1-phosphate aldolase from Escherichia coli in its tetragonal crystal form has been established at 1.92 A resolution. The homotetrameric enzyme has a molecular mass of 4 x 24 kDa and follows C(4) symmetry. The structure model is exactly symmetrical, which contradicts an observed birefringence anomaly of the crystals. The four catalytic centers are located in deep clefts at the interfaces of adjacent subunits. The zinc ion is coordinated by three histidines and one glutamate in an almost tetrahedral arrangement. In contrast to numerous other catalytically competent zinc ions, there is no water molecule in the ligand sphere. Replacement of zinc by a cobalt ion caused only small structural changes. A search through the Protein Data Bank indicated that the chain fold is novel. Sequence homology searches revealed a significant similarity to the bacterial L-ribulose-5-phosphate 4-epimerase.

PubMed: 15299567
DOI: 10.1107/S0907444996009146

実験手法

X-RAY DIFFRACTION (2 Å)