PDBsum entry 5log

Transferase

PDB id: 5log

Contents

Protein chains

222 a.a.

Ligands

SAH

LDP

Metals

_MG ×2

_CL

Waters ×297

PDB id:

5log

Name:

Transferase

Title:

Crystal structure of safc from myxococcus xanthus bound to sam

Structure:

Putative o-methyltransferase. Chain: a, b. Engineered: yes. Mutation: yes

Source:

Myxococcus xanthus. Organism_taxid: 34. Gene: safc. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.01Å R-factor: 0.178 R-free: 0.212

Authors:

S.Gerhardt,J.Netzer,O.Einsle

Key ref:

J.Siegrist et al. (2017). Functional and structural characterisation of a bacterial O-methyltransferase and factors determining regioselectivity. FEBS Lett, 591, 312-321. PubMed id: 27990630 DOI: 10.1002/1873-3468.12530

Date:

09-Aug-16 Release date: 21-Jun-17

Protein chains

Q50859  (Q50859_MYXXA) -  Putative O-methyltransferase from Myxococcus xanthus

Seq: 220 a.a.

Struc: 222 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1002/1873-3468.12530

FEBS Lett 591:312-321 (2017)

PubMed id: 27990630

Functional and structural characterisation of a bacterial O-methyltransferase and factors determining regioselectivity.

J.Siegrist, J.Netzer, S.Mordhorst, L.Karst, S.Gerhardt, O.Einsle, M.Richter, J.N.Andexer.

ABSTRACT

Mg²⁺-dependent catechol-O-methyltransferases occur in animals as well as in bacteria, fungi and plants, often with a pronounced selectivity towards one of the substrate's hydroxyl groups. Here, we show that the bacterial MxSafC exhibits excellent regioselectivity for para as well as for meta methylation, depending on the substrate's characteristics. The crystal structure of MxSafC was solved in apo and in holo form. The structure complexed with a full set of substrates clearly illustrates the plasticity of the active site region. The awareness that a wide range of factors influences the regioselectivity will aid the further development of catechol-O-methyltransferases as well as other methyltransferases as selective and efficient biocatalysts for chemical synthesis.