1OJR

L-rhamnulose-1-phosphate aldolase from Escherichia coli (mutant E192A)

1OJR の概要

• エントリーDOI: 10.2210/pdb1ojr/pdb
• 関連するPDBエントリー: 1GT7
• 分子名称: RHAMNULOSE-1-PHOSPHATE ALDOLASE, ZINC ION, PHOSPHATE ION, ... (7 entities in total)
• 機能のキーワード: lyase, aldolase (lyase), class ii, zinc enzyme, c4-tetramer, bacterial l-rhamnose metabolism, cleavage of l-rhamnulose-1- phosphate to dihydroxyacetonephosphate and l-lactaldehyde
• 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: 30918.28

構造登録者

Kroemer, M.,Merkel, I.,Schulz, G.E. (登録日: 2003-07-15, 公開日: 2003-09-11, 最終更新日: 2023-12-13)

主引用文献

Kroemer, M.,Merkel, I.,Schulz, G.E.
Structure and Catalytic Mechanism of L-Rhamnulose-1-Phosphate Aldolase.
Biochemistry, 42:10560-, 2003

PubMed Abstract: The structure of L-rhamnulose-1-phosphate aldolase has been established at 1.35 A resolution in a crystal form that was obtained by a surface mutation and has one subunit of the C(4)-symmetric tetramer in the asymmetric unit. It confirms an earlier 2.7 A resolution structure which was determined in a complicated crystal form with 20 subunits per asymmetric unit. The chain fold and the active center are similar to those of L-fuculose-1-phosphate aldolase and L-ribulose-5-phosphate 4-epimerase. The active center similarity is supported by a structural comparison of all three enzymes and by the binding mode of the inhibitor phosphoglycolohydroxamate at the site of the product dihydroxyacetone phosphate for the two aldolases. The sensitivity of the catalytic rate to several mutations and a comparison with the established mechanism of the related aldolase give rise to a putative catalytic mechanism. This mechanism involves the same binding mode of the second product L-lactaldehyde in both aldolases, except for a 180 degrees flip of the aldehyde group distinguishing between the two epimers rhamnulose and fuculose. The N-terminal domain exhibits a correlated anisotropic mobility that channels the isotropic Brownian motion into a directed movement of the catalytic base and the substrate phosphate on the N-domain toward the zinc ion and the lactaldehyde on the C-terminal domain. We suggest that this movement supports the catalysis mechanically.

PubMed: 12962479
DOI: 10.1021/BI0349266

実験手法

X-RAY DIFFRACTION (1.35 Å)