| 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
|
|
WOS Category
|
CRYSTALLOGRAPHY
BIOCHEMICAL RESEARCH METHODS
BIOPHYSICS
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
| Resource |
| DNA material |
Genomic DNA of Escherichia coli JCM 20135 (JGD07547) |
| General Microbes |
|
