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唾液酸内切酶NF在0.98埃分辨率下的结构分析。

Structure analysis of endosialidase NF at 0.98 A resolution.

作者信息

Schulz Eike C, Neumann Piotr, Gerardy-Schahn Rita, Sheldrick George M, Ficner Ralf

机构信息

Abteilung für Molekulare Strukturbiologie, Institut für Mikrobiologie und Genetik, Georg-August-Universität Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany.

出版信息

Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):176-80. doi: 10.1107/S0907444909048720. Epub 2010 Jan 22.

Abstract

Endosialidase NF (endoNF) is a bacteriophage-derived endosialidase that specifically degrades alpha-2,8-linked polysialic acid. The structure of a new crystal form of endoNF in complex with sialic acid has been refined at 0.98 A resolution. The 210 kDa homotrimeric multi-domain enzyme displays outstanding stability and resistance to SDS. Even at atomic resolution, only a minor fraction of side chains possess alternative conformations. However, multiple conformations of an active-site residue imply that it has an important catalytic function in the cleavage mechanism of polysialic acid.

摘要

内切唾液酸酶NF(endoNF)是一种源自噬菌体的内切唾液酸酶,可特异性降解α-2,8连接的多聚唾液酸。与唾液酸复合的endoNF新晶体形式的结构已在0.98埃分辨率下进行了优化。这种210 kDa的同三聚体多结构域酶表现出出色的稳定性和对SDS的抗性。即使在原子分辨率下,也只有一小部分侧链具有替代构象。然而,一个活性位点残基的多种构象表明它在多聚唾液酸的切割机制中具有重要的催化功能。

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