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具有短天然外显肽和活性N端催化半胱氨酸的小型RecA内含肽的主链归属

Backbone assignments of mini-RecA intein with short native exteins and an active N-terminal catalytic cysteine.

作者信息

Pearson C Seth, Belfort Georges, Belfort Marlene, Shekhtman Alexander

机构信息

Howard P. Isermann Department of Chemical and Biological Engineering and The Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA.

Department of Biological Sciences and The RNA Institute, University at Albany, Albany, NY, 12222, USA.

出版信息

Biomol NMR Assign. 2015 Oct;9(2):235-8. doi: 10.1007/s12104-014-9581-z. Epub 2014 Oct 4.

Abstract

The backbone resonance assignments of an engineered splicing-inactive mini-RecA intein based on triple resonance experiments with [(13)C,(15)N]-labeled protein are reported. The construct contains inactivating mutations specifically designed to retain most catalytic residues, especially those that are potentially metal-coordinating. The assignments are essential for protein structure determination of a precursor with an active N-terminal catalytic cysteine and for investigation of the atomic details of splicing.

摘要

报道了基于对[(13)C,(15)N]标记蛋白质进行三重共振实验的工程化剪接失活型迷你RecA内含肽的主链共振归属。该构建体包含专门设计的失活突变,以保留大多数催化残基,特别是那些可能参与金属配位的残基。这些归属对于具有活性N端催化半胱氨酸的前体的蛋白质结构测定以及剪接原子细节的研究至关重要。

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