Preparation, crystallization and preliminary X-ray analysis of protein YtlP from Bacillus subtilis

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt 10):967-9. doi: 10.1107/S174430910603199X. Epub 2006 Sep 19.

Abstract

Bacillus subtilis YtlP is a protein that is predicted to belong to the bacterial and archael 2'-5' RNA-ligase family. It contains 183 residues and two copies of the HXTX sequence motif conserved among proteins belonging to this family. In order to determine the structure of YtlP and to compare it with the paralogue YjcG and identified 2'-5' RNA ligases, the gene ytlP was amplified from B. subtilis genomic DNA and cloned into expression vector pET-21a. The soluble protein was produced in Escherichia coli, purified to homogeneity and crystals suitable for X-ray analysis were obtained. The crystal diffracted to 2.0 A and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 34.16, b = 48.54, c = 105.75 A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacillus subtilis / chemistry
  • Bacillus subtilis / enzymology*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Polynucleotide Ligases / chemistry*
  • Polynucleotide Ligases / genetics
  • Polynucleotide Ligases / isolation & purification
  • Sequence Alignment

Substances

  • Bacterial Proteins
  • Polynucleotide Ligases