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5MBT

CeuE (H227L, Y288F variant) a periplasmic protein from Campylobacter jejuni

Summary for 5MBT
Entry DOI10.2210/pdb5mbt/pdb
DescriptorEnterochelin uptake periplasmic binding protein (2 entities in total)
Functional Keywordsperiplasmic, iron-uptake, tetradentate, siderophore, mutation, metal transport
Biological sourceCampylobacter jejuni
Total number of polymer chains3
Total formula weight96122.99
Authors
Wilde, E.J.,Blagova, E.V.,Hughes, A.,Raines, D.J.,Moroz, O.V.,Turkenburg, J.P.,Duhme-Klair, A.-K.,Wilson, K.S. (deposition date: 2016-11-08, release date: 2017-04-12, Last modification date: 2024-01-17)
Primary citationWilde, E.J.,Hughes, A.,Blagova, E.V.,Moroz, O.V.,Thomas, R.P.,Turkenburg, J.P.,Raines, D.J.,Duhme-Klair, A.K.,Wilson, K.S.
Interactions of the periplasmic binding protein CeuE with Fe(III) n-LICAM(4-) siderophore analogues of varied linker length.
Sci Rep, 7:45941-45941, 2017
Cited by
PubMed Abstract: Bacteria use siderophores to mediate the transport of essential Fe(III) into the cell. In Campylobacter jejuni the periplasmic binding protein CeuE, an integral part of the Fe(III) transport system, has adapted to bind tetradentate siderophores using a His and a Tyr side chain to complete the Fe(III) coordination. A series of tetradentate siderophore mimics was synthesized in which the length of the linker between the two iron-binding catecholamide units was increased from four carbon atoms (4-LICAM) to five, six and eight (5-, 6-, 8-LICAM, respectively). Co-crystal structures with CeuE showed that the inter-planar angles between the iron-binding catecholamide units in the 5-, 6- and 8-LICAM structures are very similar (111°, 110° and 110°) and allow for an optimum fit into the binding pocket of CeuE, the inter-planar angle in the structure of 4-LICAM is significantly smaller (97°) due to restrictions imposed by the shorter linker. Accordingly, the protein-binding affinity was found to be slightly higher for 5- compared to 4-LICAM but decreases for 6- and 8-LICAM. The optimum linker length of five matches that present in natural siderophores such as enterobactin and azotochelin. Site-directed mutagenesis was used to investigate the relative importance of the Fe(III)-coordinating residues H227 and Y288.
PubMed: 28383577
DOI: 10.1038/srep45941
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

229380

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