PDBsum entry 6l2f

Metal binding protein

PDB id: 6l2f

Contents

Protein chains

118 a.a.

Ligands

_CU ×2

P33

MES

Waters ×226

PDB id:

6l2f

Name:

Metal binding protein

Title:

Crystal structure of a cupin protein (tm1459, h54ah58a mutant) in copper (cu) substituted form

Structure:

Cupin_2 domain-containing protein. Chain: a, b. Engineered: yes

Source:

Thermotoga maritima msb8. Organism_taxid: 243274. Strain: msb8. Gene: tm_1459. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.23Å R-factor: not given

Authors:

N.Fujieda,H.Ichihashi,Y.Nishikawa,G.Kurisu,S.Itoh

Key ref:

N.Fujieda et al. (2020). Cupin Variants as a Macromolecular Ligand Library for Stereoselective Michael Addition of Nitroalkanes. Angew Chem Int Ed Engl, 59, 7717-7720. PubMed id: 32073197 DOI: 10.1002/anie.202000129

Date:

03-Oct-19 Release date: 01-Apr-20

Protein chains

Q9X1H0  (Q9X1H0_THEMA) -  Cupin type-2 domain-containing protein from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

Seq: 114 a.a.

Struc: 119 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1002/anie.202000129

Angew Chem Int Ed Engl 59:7717-7720 (2020)

PubMed id: 32073197

Cupin Variants as a Macromolecular Ligand Library for Stereoselective Michael Addition of Nitroalkanes.

N.Fujieda, H.Ichihashi, M.Yuasa, Y.Nishikawa, G.Kurisu, S.Itoh.

ABSTRACT

Cupin superfamily proteins (TM1459) work as a macromolecular ligand framework with a double-stranded β-barrel structure ligating to a Cu ion through histidine side chains. Variegating the first coordination sphere of TM1459 revealed that H52A and H54A/H58A mutants effectively catalyzed the diastereo- and enantioselective Michael addition reaction of nitroalkanes to an α,β-unsaturated ketone. Moreover, calculated substrate docking signified C106N and F104W single-point mutations, which inverted the diastereoselectivity of H52A and further improved the stereoselectivity of H54A/H58A, respectively.