1ILD

OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT pH 4.6

1ILD の概要

• エントリーDOI: 10.2210/pdb1ild/pdb
• 関連するPDBエントリー: 1FW2 1FW3 1QD5 1QD6
• 分子名称: OUTER MEMBRANE PHOSPHOLIPASE A, octyl beta-D-glucopyranoside, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• 機能のキーワード: anti-parallel beta barrel, membrane phospholipase, membrane protein, serine hydrolase, n156a, hydrolase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane; Multi-pass membrane protein: P0A921
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33310.22

構造登録者

Snijder, H.J.,Van Eerde, J.H.,Kingma, R.L.,Kalk, K.H.,Dekker, N.,Egmond, M.R.,Dijkstra, B.W. (登録日: 2001-05-08, 公開日: 2001-10-03, 最終更新日: 2023-08-16)

主引用文献

Snijder, H.J.,Van Eerde, J.H.,Kingma, R.L.,Kalk, K.H.,Dekker, N.,Egmond, M.R.,Dijkstra, B.W.
Structural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A: function of the Asn-His interaction in the catalytic triad.
Protein Sci., 10:1962-1969, 2001

PubMed Abstract: Outer membrane phospholipase A (OMPLA) from Escherichia coli is an integral-membrane enzyme with a unique His-Ser-Asn catalytic triad. In serine proteases and serine esterases usually an Asp occurs in the catalytic triad; its role has been the subject of much debate. Here the role of the uncharged asparagine in the active site of OMPLA is investigated by structural characterization of the Asn156Ala mutant. Asparagine 156 is not involved in maintaining the overall active-site configuration and does not contribute significantly to the thermal stability of OMPLA. The active-site histidine retains an active conformation in the mutant notwithstanding the loss of the hydrogen bond to the asparagine side chain. Instead, stabilization of the correct tautomeric form of the histidine can account for the observed decrease in activity of the Asn156Ala mutant.

PubMed: 11567087
DOI: 10.1110/ps.17701

実験手法

X-RAY DIFFRACTION (2.8 Å)