ISDA: 6L2E

Deposition Date 2019-10-03

Release Date 2020-04-01

Last Version Date 2024-11-13

Entry Detail

PDB ID:

6L2E

Keywords:

METAL BINDING PROTEIN

Title:

Crystal structure of a cupin protein (tm1459, H52A mutant) in copper (Cu) substituted form

Biological Source:

Source Organism(s):

Thermotoga maritima MSB8 (Taxon ID: 243274)

Expression System(s):

Escherichia coli bl21(de3)

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

1.20 Å

R-Value Free:

0.17

R-Value Work:

0.14

R-Value Observed:

0.14

Space Group:

P 21 21 21

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Macromolecular Entities

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:Cupin_2 domain-containing pro
Gene (Uniprot):Tmari_1465
Chain IDs:A, B
Chain Length:118
Number of Molecules:2
Biological Source:Thermotoga maritima MSB8

UniProt ID:Q9X1H0 Pfam ID:PF07883

Modified Residue

Compound ID	Chain ID	Parent Comp ID	Details	2D Image
CSD	A	CYS	modified residue

Ligand Molecules

MES

Primary Citation

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

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

Angew. Chem. Int. Ed. Engl. 59 7717 7720 (2020)

PMID: 32073197 DOI: 10.1002/anie.202000129

Abstact

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.

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Protein

Chemical

Disease

Primary Citation of related structures

Abstact

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