7yr9

Publication Abstract from PubMed

Iron-sulfur clusters are prosthetic groups of proteins involved in various biological processes. However, details of the immature state of the iron-sulfur cluster into proteins have not yet been elucidated. We report here the first structural analysis of the Zn-containing form of a Rieske-type iron-sulfur protein, PetA, from Thermochromatium tepidum (TtPetA) by X-ray crystallography and small-angle X-ray scattering analysis. The Zn-containing form of TtPetA was indicated to be a dimer in solution. The zinc ion adopts a regular tetra-coordination with two chloride ions and two cysteine residues. Only a histidine residue in the cluster-binding site exhibited a conformational difference from the [2Fe-2S] containing form. The Zn-containing structure indicates that the conformation of the cluster binding site is already constructed and stabilized before insertion of [2Fe-2S]. The binding mode of ZnCl(2), similar to the [2Fe-2S] cluster, suggests that the zinc ions might be involved in the insertion of the [2Fe-2S] cluster.

Structure of a putative immature form of a Rieske-type iron-sulfur protein in complex with zinc chloride.,Tsutsumi E, Niwa S, Takeda R, Sakamoto N, Okatsu K, Fukai S, Ago H, Nagao S, Sekiguchi H, Takeda K Commun Chem. 2023 Sep 9;6(1):190. doi: 10.1038/s42004-023-01000-6. PMID:37689761^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.