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PDBsum entry 5o4h
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PDB id:
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Transferase
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Title:
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Hcgc from methanococcus maripaludis cocrystallized with sam and pyridinol
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Structure:
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Hcgc. Chain: a, b, c, d. Engineered: yes. Other_details: a his-tagged has been placed in thE C-terminal of the construct
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Source:
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Methanococcus maripaludis s2. Organism_taxid: 267377. Cell_line: /. Gene: mmp1498. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: star.
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Resolution:
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1.75Å
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R-factor:
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0.169
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R-free:
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0.193
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Authors:
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T.Wagner,L.Bai,T.Xu,X.Hu,U.Ermler,S.Shima
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Key ref:
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L.Bai
et al.
(2017).
A Water-Bridged H-Bonding Network Contributes to the Catalysis of the SAM-Dependent C-Methyltransferase HcgC.
Angew Chem Int Ed Engl,
56,
10806-10809.
PubMed id:
DOI:
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Date:
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29-May-17
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Release date:
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19-Jul-17
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PROCHECK
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Headers
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References
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Q6LX54
(Q6LX54_METMP) -
Uncharacterized protein from Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)
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Seq:
Struc:
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260 a.a.
260 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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DOI no:
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Angew Chem Int Ed Engl
56:10806-10809
(2017)
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PubMed id:
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A Water-Bridged H-Bonding Network Contributes to the Catalysis of the SAM-Dependent C-Methyltransferase HcgC.
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L.Bai,
T.Wagner,
T.Xu,
X.Hu,
U.Ermler,
S.Shima.
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ABSTRACT
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[Fe]-hydrogenase hosts an iron-guanylylpyridinol (FeGP) cofactor. The FeGP
cofactor contains a pyridinol ring substituted with GMP, two methyl groups, and
an acylmethyl group. HcgC, an enzyme involved in FeGP biosynthesis, catalyzes
methyl transfer from S-adenosylmethionine (SAM) to C3 of
6-carboxymethyl-5-methyl-4-hydroxy-2-pyridinol (2). We report on the ternary
structure of HcgC/S-adenosylhomocysteine (SAH, the demethylated product of SAM)
and 2 at 1.7 Å resolution. The proximity of C3 of substrate 2 and the S atom
of SAH indicates a catalytically productive geometry. The hydroxy and carboxy
groups of substrate 2 are hydrogen-bonded with I115 and T179, as well as through
a series of water molecules linked with polar and a few protonatable groups.
These interactions stabilize the deprotonated state of the hydroxy groups and a
keto form of substrate 2, through which the nucleophilicity of C3 is increased
by resonance effects. Complemented by mutational analysis, a structure-based
catalytic mechanism was proposed.
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