Literature DB >> 24192372

Cloning, expression, purification, crystallization and preliminary crystallographic analysis of the putative NlpC/P60 endopeptidase, TTHA0266, from Thermus thermophilus HB8.

Jaslyn E M M Wong1, Mickael Blaise.   

Abstract

Autolysins belong to a protein family involved in peptidoglycan degradation and remodelling. Within this family, NlpC/P60 endopeptidases are involved in the hydrolysis of the peptide arm of peptidoglycan. In this work, the putative NlpC/P60 endopeptidase TTHA0266 from Thermus thermophilus HB8 was overexpressed, purified and crystallized. The crystals diffracted to 2.4 Å resolution and belonged to the hexagonal space group P6(1), with unit-cell parameters a = b = 71.19, c = 198.68 Å, γ = 120°. Selenomethionine-substituted protein was crystallized and the structure was solved by single-wavelength anomalous dispersion.

Entities:  

Keywords:  LysM; NlpC/P60; TTHA0266; Thermus thermophilus; autolysin; endopeptidases; peptidoglycan

Mesh：

Substances：

Year:  2013        PMID： 24192372      PMCID： PMC3818056          DOI： 10.1107/S1744309113027164

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN： 1744-3091


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  1 in total

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