RRC ID 31850
Author Kobayashi K, Suzuki T, Dohmae N, Ishitani R, Nureki O.
Title Crystallization and preliminary X-ray crystallographic analysis of YfcM: an important factor for EF-P hydroxylation.
Journal Acta Crystallogr F Struct Biol Commun
Abstract Elongation factor P (EF-P) plays an essential role in the translation of polyproline-containing proteins in bacteria. It becomes functional by the post-translational modification of its highly conserved lysine residue. It is first β-lysylated by PoxA and then hydroxylated by YfcM. In this work, the YfcM protein from Escherichia coli was overexpressed, purified and crystallized. The crystal of YfcM was obtained by the in situ proteolysis crystallization method and diffracted X-rays to 1.45 Å resolution. It belonged to space group C2, with unit-cell parameters a = 124.4, b = 37.0, c = 37.6 Å, β = 101.2°. The calculated Matthews coefficient (VM) of the crystal was 1.91 Å(3) Da(-1), indicating that one YfcM molecule is present in the asymmetric unit with a solvent content of 35.7%.
Volume 70(Pt 9)
Pages 1236-9
Published 2014-9-1
DOI 10.1107/S2053230X14015726
PII S2053230X14015726
PMID 25195899
PMC PMC4157426
MeSH Amino Acid Sequence Base Sequence Crystallization Crystallography, X-Ray / methods* DNA Primers Escherichia coli Proteins / chemistry* Hydroxylation Mixed Function Oxygenases / chemistry* Molecular Sequence Data Peptide Elongation Factors / chemistry* Protein Conformation Proteolysis
IF 0.968
Times Cited 3
DNA material Genomic DNA of Escherichia coli JCM 20135 (JGD07547)
General Microbes