PDBsum entry 3wv7

Transferase

PDB id: 3wv7

Contents

Protein chains

201 a.a.

Ligands

ADP

Waters ×366

PDB id:

3wv7

Name:

Transferase

Title:

Hcge from methanothermobacter marburgensis

Structure:

Hmd co-occurring protein hcge. Chain: a, b, c. Engineered: yes

Source:

Methanothermobacter marburgensis. Organism_taxid: 79929. Strain: dsm 2133 / 14651 / nbrc 100331 / ocm 82 / marburg. Gene: hcge, mtbma_c15310. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.60Å R-factor: 0.167 R-free: 0.199

Authors:

T.Fujishiro,U.Ermler,S.Shima

Key ref:

T.Fujishiro et al. (2015). Protein-pyridinol thioester precursor for biosynthesis of the organometallic acyl-iron ligand in [Fe]-hydrogenase cofactor. Nat Commun, 6, 6895. PubMed id: 25882909 DOI: 10.1038/ncomms7895

Date:

16-May-14 Release date: 29-Apr-15

Protein chains

D9PY12  (D9PY12_METTM) -  Hmd co-occurring protein HcgE from Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)

Seq: 212 a.a.

Struc: 201 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.7.- - ?????

DOI no: 10.1038/ncomms7895

Nat Commun 6:6895 (2015)

PubMed id: 25882909

Protein-pyridinol thioester precursor for biosynthesis of the organometallic acyl-iron ligand in [Fe]-hydrogenase cofactor.

T.Fujishiro, J.Kahnt, U.Ermler, S.Shima.

ABSTRACT

The iron-guanylylpyridinol (FeGP) cofactor of [Fe]-hydrogenase contains a prominent iron centre with an acyl-Fe bond and is the only acyl-organometallic iron compound found in nature. Here, we identify the functions of HcgE and HcgF, involved in the biosynthesis of the FeGP cofactor using structure-to-function strategy. Analysis of the HcgE and HcgF crystal structures with and without bound substrates suggest that HcgE catalyses the adenylylation of the carboxy group of guanylylpyridinol (GP) to afford AMP-GP, and subsequently HcgF catalyses the transesterification of AMP-GP to afford a Cys (HcgF)-S-GP thioester. Both enzymatic reactions are confirmed by in vitro assays. The structural data also offer plausible catalytic mechanisms. This strategy of thioester activation corresponds to that used for ubiquitin activation, a key event in the regulation of multiple cellular processes. It further implicates a nucleophilic attack onto the acyl carbon presumably via an electron-rich Fe(0)- or Fe(I)-carbonyl complex in the Fe-acyl formation.