1UCO

HEN EGG-WHITE LYSOZYME, LOW HUMIDITY FORM

1UCO の概要

• エントリーDOI: 10.2210/pdb1uco/pdb
• 分子名称: LYSOZYME (2 entities in total)
• 機能のキーワード: enzyme-monoclinic form, hydrolase, o-glycosyl, hydrolase (o-glycosyl)
• 由来する生物種: Gallus gallus (chicken)
• 細胞内の位置: Secreted: P00698
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28662.32

構造登録者

Nagendra, H.G.,Sudarsanakumar, C.,Vijayan, M. (登録日: 1995-12-31, 公開日: 1996-07-11, 最終更新日: 2024-10-16)

主引用文献

Nagendra, H.G.,Sudarsanakumar, C.,Vijayan, M.
An X-ray analysis of native monoclinic lysozyme. A case study on the reliability of refined protein structures and a comparison with the low-humidity form in relation to mobility and enzyme action.
Acta Crystallogr.,Sect.D, 52:1067-1074, 1996

PubMed Abstract: The atomic models of native monoclinic lysozyme obtained by refinement at Bangalore and elsewhere [Young, Dewan, Nave & Tilton (1993). J. Appl. Cryst. 26, 309-319] differed significantly in the flexible regions of the protein molecule. The two models were reconciled starting from regions where they were in reasonable agreement to produce an improved model which yielded an R value of 0.169 for 12 816 observed reflections in the 10-2 A resolution range. The reconciled model was compared with the structure of the 88% relative humidity form obtained through a water-mediated transformation [Madhusudan, Kodandapani & Vijayan (1993). Acta Cryst. D49, 234-245]. Parts of the flexible regions of the molecule register significant movements during the transformation. The changes resulting from the transformation from the native to the low-humidity forms are pronounced in many of the side chains in the active-site region, thus indicating the relationship between hydration, mobility and enzyme action. The fact that the overall changes in molecular geometry resulting from water-mediated transformation are similar to those which occur during enzyme action, further emphasizes this relationship.

PubMed: 15299565
DOI: 10.1107/S0907444996002181

実験手法

X-RAY DIFFRACTION (2 Å)