1K6A

Structural studies on the mobility in the active site of the Thermoascus aurantiacus xylanase I

「1FXM」から置き換えられました

1K6A の概要

• エントリーDOI: 10.2210/pdb1k6a/pdb
• 関連するPDBエントリー: 1fxm 1tax
• 分子名称: xylanase I (2 entities in total)
• 機能のキーワード: alternate conformations, active site mobility, hydrolase
• 由来する生物種: Thermoascus aurantiacus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32907.74

構造登録者

Lo Leggio, L.,Kalogiannis, S.,Eckert, K.,Teixeira, S.C.M.,Bhat, M.K.,Andrei, C.,Pickersgill, R.W.,Larsen, S. (登録日: 2001-10-15, 公開日: 2002-07-03, 最終更新日: 2024-11-06)

主引用文献

Lo Leggio, L.,Kalogiannis, S.,Eckert, K.,Teixeira, S.C.,Bhat, M.K.,Andrei, C.,Pickersgill, R.W.,Larsen, S.
Substrate specificity and subsite mobility in T. aurantiacus xylanase 10A.
FEBS LETT., 509:303-308, 2001

PubMed Abstract: The substrate specificity of Thermoascus aurantiacus xylanase 10A (TAX) has been investigated both biochemically and structurally. High resolution crystallographic analyses at 291 K and 100 K of TAX complexes with xylobiose show that the ligand is in its alpha anomeric conformation and provide a rationale for specificity on p-nitrophenyl glycosides at the -1 and -2 subsites. Trp 275, which is disordered in uncomplexed structures, is stabilised by its interaction with xylobiose. Two structural subsets in family 10 are identified, which differ by the presence or absence of a short helical stretch in the eighth betaalpha-loop of the TIM barrel, the loop bearing Trp 275. This structural difference is discussed in the context of Trp 275 mobility and xylanase function.

PubMed: 11741607
DOI: 10.1016/S0014-5793(01)03177-5

実験手法

X-RAY DIFFRACTION (1.14 Å)