7BHC
Escherichia coli YtfE E125L
Summary for 7BHC
Entry DOI | 10.2210/pdb7bhc/pdb |
Descriptor | Iron-sulfur cluster repair protein YtfE, FE (III) ION, OXYGEN ATOM, ... (5 entities in total) |
Functional Keywords | di-iron, metal binding protein |
Biological source | Escherichia coli (strain K12) |
Total number of polymer chains | 2 |
Total formula weight | 50032.47 |
Authors | Silva, L.S.O.,Matias, P.M.,Romao, C.V.,Saraiva, L.M. (deposition date: 2021-01-11, release date: 2021-04-21, Last modification date: 2024-01-31) |
Primary citation | Silva, L.S.O.,Matias, P.M.,Romao, C.V.,Saraiva, L.M. Structural Basis of RICs Iron Donation for Iron-Sulfur Cluster Biogenesis. Front Microbiol, 12:670681-670681, 2021 Cited by PubMed Abstract: YtfE is a di-iron protein of the widespread Repair of Iron Centers proteins (RIC) family that has the capacity to donate iron, which is a crucial component of the biogenesis of the ubiquitous family of iron-sulfur proteins. In this work we identify in a previously unrecognized link between the YtfE protein and the major bacterial system for iron-sulfur cluster (ISC) assembly. We show that YtfE establishes protein-protein interactions with the scaffold IscU, where the transient cluster is formed, and the cysteine desulfurase IscS. Moreover, we found that promotion by YtfE of the formation of an Fe-S cluster in IscU requires two glutamates, E125 and E159 in YtfE. Both glutamates form part of the entrance of a protein channel in YtfE that links the di-iron center to the surface. In particular, E125 is crucial for the exit of iron, as a single mutation to leucine closes the channel rendering YtfE inactive for the build-up of Fe-S clusters. Hence, we provide evidence for the key role of RICs as bacterial iron donor proteins involved in the biogenesis of Fe-S clusters. PubMed: 33995335DOI: 10.3389/fmicb.2021.670681 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.87 Å) |
Structure validation
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