8B7X

X-ray structure of the CeuE Homologue from Geobacillus stearothermophilus - apo form.

Summary for 8B7X

• Entry DOI: 10.2210/pdb8b7x/pdb
• Descriptor: Siderophore ABC transporter substrate-binding protein, O-(O-(2-AMINOPROPYL)-O'-(2-METHOXYETHYL)POLYPROPYLENE GLYCOL 500), SULFATE ION, ... (4 entities in total)
• Functional Keywords: periplasmic, siderophore binding, bacterial, apo protein., metal transport
• Biological source: Geobacillus stearothermophilus
• Total number of polymer chains: 1
• Total formula weight: 34079.82

Authors

Wilson, K.S.,Duhme-Klair, A.K.,Blagova, E.V.,Bennett, M. (deposition date: 2022-10-03, release date: 2023-07-12, Last modification date: 2024-02-07)

Primary citation

Blagova, E.V.,Miller, A.H.,Bennett, M.,Booth, R.L.,Dodson, E.J.,Duhme-Klair, A.K.,Wilson, K.S.
Thermostable homologues of the periplasmic siderophore-binding protein CeuE from Geobacillus stearothermophilus and Parageobacillus thermoglucosidasius.
Acta Crystallogr D Struct Biol, 79:694-705, 2023

PubMed Abstract: Siderophore-binding proteins from two thermophilic bacteria, Geobacillus stearothermophilus and Parageobacillus thermoglucosidasius, were identified from a search of sequence databases, cloned and overexpressed. They are homologues of the well characterized protein CjCeuE from Campylobacter jejuni. The iron-binding histidine and tyrosine residues are conserved in both thermophiles. Crystal structures were determined of the apo proteins and of their complexes with iron(III)-azotochelin and its analogue iron(III)-5-LICAM. The thermostability of both homologues was shown to be about 20°C higher than that of CjCeuE. Similarly, the tolerance of the homologues to the organic solvent dimethylformamide (DMF) was enhanced, as reflected by the respective binding constants for these ligands measured in aqueous buffer at pH 7.5 in the absence and presence of 10% and 20% DMF. Consequently, these thermophilic homologues offer advantages in the development of artificial metalloenzymes using the CeuE family.

PubMed: 37428843
DOI: 10.1107/S2059798323004473

Experimental method

X-RAY DIFFRACTION (1.42 Å)