 |
PDBsum entry 5d4t
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Unknown function
|
PDB id
|
|
|
|
5d4t
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Unknown function
|
|
|
Title:
|
|
Semet-labelled hcgc from methanocaldococcus jannaschii in space group p212121
|
|
Structure:
|
|
Uncharacterized protein mj0489. Chain: a, b, c, d, e, f, g, h. Fragment: rossmann-like domain, residues 2-268. Synonym: hcgc. Engineered: yes
|
|
Source:
|
|
Methanocaldococcus jannaschii. Organism_taxid: 2190. Gene: mj0489. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
|
|
Resolution:
|
|
|
2.90Å
|
R-factor:
|
0.229
|
R-free:
|
0.259
|
|
|
Authors:
|
|
T.Fujishiro,U.Ermler,S.Shima
|
|
Key ref:
|
|
T.Fujishiro
et al.
(2016).
Identification of HcgC as a SAM-Dependent Pyridinol Methyltransferase in [Fe]-Hydrogenase Cofactor Biosynthesis.
Angew Chem Int Ed Engl,
55,
9648-9651.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
09-Aug-15
|
Release date:
|
20-Jul-16
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
Q57913
(Y489_METJA) -
Uncharacterized protein MJ0489 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
|
|
|
|
Seq:
Struc:
|
|
|
|
268 a.a.
243 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Angew Chem Int Ed Engl
55:9648-9651
(2016)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Identification of HcgC as a SAM-Dependent Pyridinol Methyltransferase in [Fe]-Hydrogenase Cofactor Biosynthesis.
|
|
T.Fujishiro,
L.Bai,
T.Xu,
X.Xie,
M.Schick,
J.Kahnt,
M.Rother,
X.Hu,
U.Ermler,
S.Shima.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
Previous retrosynthetic and isotope-labeling studies have indicated that
biosynthesis of the iron guanylylpyridinol (FeGP) cofactor of [Fe]-hydrogenase
requires a methyltransferase. This hypothetical enzyme covalently attaches the
methyl group at the 3-position of the pyridinol ring. We describe the
identification of HcgC, a gene product of the hcgA-G cluster responsible for
FeGP cofactor biosynthesis. It acts as an S-adenosylmethionine (SAM)-dependent
methyltransferase, based on the crystal structures of HcgC and the HcgC/SAM and
HcgC/S-adenosylhomocysteine (SAH) complexes. The pyridinol substrate,
6-carboxymethyl-5-methyl-4-hydroxy-2-pyridinol, was predicted based on
properties of the conserved binding pocket and substrate docking simulations.
For verification, the assumed substrate was synthesized and used in a kinetic
assay. Mass spectrometry and NMR analysis revealed
6-carboxymethyl-3,5-dimethyl-4-hydroxy-2-pyridinol as the reaction product,
which confirmed the function of HcgC.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
