5WQR

High resolution structure of high-potential iron-sulfur protein in the reduced state

Summary for 5WQR

• Entry DOI: 10.2210/pdb5wqr/pdb
• Related: 5WQQ
• Descriptor: High-potential iron-sulfur protein, IRON/SULFUR CLUSTER, SULFATE ION, ... (5 entities in total)
• Functional Keywords: iron-sulfur protein, metal-binding protein, metal binding protein
• Biological source: Thermochromatium tepidum
• Total number of polymer chains: 1
• Total formula weight: 9902.09

Authors

Ohno, H.,Takeda, K.,Niwa, S.,Tsujinaka, T.,Hanazono, Y.,Hirano, Y.,Miki, K. (deposition date: 2016-11-28, release date: 2017-06-07, Last modification date: 2023-11-08)

Primary citation

Ohno, H.,Takeda, K.,Niwa, S.,Tsujinaka, T.,Hanazono, Y.,Hirano, Y.,Miki, K.
Crystallographic characterization of the high-potential iron-sulfur protein in the oxidized state at 0.8 angstrom resolution
PLoS ONE, 12:e0178183-e0178183, 2017

PubMed Abstract: High-potential iron-sulfur protein (HiPIP) is a soluble electron carrier protein of photosynthetic bacteria with an Fe4S4 cluster. Although structural changes accompanying the electron transfer are important for understanding of the functional mechanism, the changes have not been clarified in sufficient detail. We previously reported the high-resolution crystal structures of HiPIP from a thermophilic purple bacterium Thermochromatium tepidum in the reduced state. In order to perform a detailed comparison between the structures in different redox states, the oxidized structure should also be revealed at high resolution. Therefore, in the present study we performed a crystallographic analysis of oxidized HiPIP and a structural comparison with the reduced form at a high resolution of 0.8 Å. The comparison highlighted small but significant contraction in the iron-sulfur cluster. The changes in Fe-S bond lengths were similar to that predicted by theoretical calculation, although some discrepancies were also found. Almost distances between the sulfur atoms of the iron-sulfur cluster and the protein environment are elongated upon the oxidation. Positional changes of hydrogen atoms in the protein environment, such as on the amide-hydrogen of Cys75 in the proximity of the iron-sulfur cluster, were also observed in the accurate analyses. None of the water molecules exhibited significant changes in position or anisotropy of atomic displacement parameter between the two states, while the orientations of some water molecules were different.

PubMed: 28542634
DOI: 10.1371/journal.pone.0178183

Experimental method

X-RAY DIFFRACTION (0.8 Å)