Crystal structure of the ancient, Fe-S scaffold IscA reveals a novel protein fold.

Biochemistry

Department of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA.

Published: January 2004

IscA belongs to an ancient family of proteins responsible for iron-sulfur cluster assembly in essential metabolic pathways preserved throughout evolution. We report here the 2.3 A resolution crystal structure of Escherichia coli IscA, a novel fold in which mixed beta-sheets form a compact alpha-beta sandwich domain. In contrast to the highly mobile secondary structural elements within the bacterial Fe-S scaffold protein IscU, a protein which is thought to have a similar function, the great majority of the amino acids that are conserved in IscA homologues are located in elements that constitute a well-ordered fold. However, the 10-residue C-terminal tail segment that contains two invariant cysteines critical for the Fe-S-binding function of a cyanobacterial (Synechocystis PCC) IscA homologue is not ordered in our structure. In addition, the crystal packing reveals a helical assembly that is constructed from two possible tetrameric oligomers of IscA.

Download full-text PDF

Source
http://dx.doi.org/10.1021/bi035440sDOI Listing

Publication Analysis

Top Keywords

crystal structure
8
fe-s scaffold
8
isca
6
structure ancient
4
ancient fe-s
4
scaffold isca
4
isca reveals
4
reveals novel
4
novel protein
4
protein fold
4

Similar Publications

Recent Progress and Advances of Perovskite Crystallization in Carbon-Based Printable Mesoscopic Solar Cells.

Adv Mater

January 2025

Michael Grätzel Center for Mesoscopic Solar Cells Wuhan National Laboratory for Optoelectronics Key Laboratory of Materials Chemistry for Energy Conversion and Storage of Ministry of Education, Huazhong University of Science and Technology, Wuhan, Hubei, 430074, P. R. China.

Carbon-based printable mesoscopic solar cells (p-MPSCs) offer significant advantages for industrialization due to their simple fabrication process, low cost, and scalability. Recently, the certified power conversion efficiency of p-MPSCs has exceeded 22%, drawing considerable attention from the community. However, the key challenge in improving device performance is achieving uniform and high-quality perovskite crystallization within the mesoporous structure.

View Article and Find Full Text PDF

Biosynthesis and activity of Zn-MnO nanocomposite in vitro with molecular docking studies against multidrug resistance bacteria and inflammatory activators.

Sci Rep

January 2025

Department of Hematology/Oncology, Yousef Abdulatif Jameel Scientific Chair of Prophetic Medicine Application, Faculty of Medicine, King Abdulaziz University, Jeddah, 21589, Kingdom of Saudi Arabia.

This study investigated the green synthesis of Zn-MnO nanocomposites via the fungus Penicillium rubens. Herein, the synthesized Zn-MnO nanocomposites were confirmed by UV-spectrophotometry with a top peak (370 nm). Transmission electron microscopy confirmed irregular particles with a spherical-like shape ranging from 25.

View Article and Find Full Text PDF

Competitive displacement of lipoprotein lipase from heparan sulfate is orchestrated by a disordered acidic cluster in GPIHBP1.

J Lipid Res

January 2025

Finsen Laboratory, Copenhagen University Hospital - Rigshospitalet, Copenhagen, Denmark; Biotech Research and Innovation Centre, University of Copenhagen, Copenhagen, Denmark. Electronic address:

Movement of lipoprotein lipase (LPL) from myocytes or adipocytes to the capillary lumen is essential for intravascular lipolysis and plasma triglyceride homeostasis-low LPL activity in the capillary lumen causes hypertriglyceridemia. The trans-endothelial transport of LPL depends on ionic interactions with GPIHBP1's intrinsically disordered N-terminal tail, which harbors two acidic clusters at positions 5-12 and 19-30. This polyanionic tail provides a molecular switch that controls LPL detachment from heparan sulfate proteoglycans (HSPGs) by competitive displacement.

View Article and Find Full Text PDF

The present study intended to investigate the properties of collagen peptide (CP)-astragaloside (AG) nanocomplexes (CPANs) improved oxidized hydroxypropyl starch (OHS)/chitosan (CS) (OC) film and to explore the preservation of chilled beef. The results indicated that AG significantly enhanced the stability, antioxidant capacity, and antibacterial properties of CP through mechanisms like static quenching and hydrophobic interactions. The incorporation of CPANs improved thickness, swellability, and water vapor blocking, UV-blocking and mechanical properties, antioxidant and antibacterial activity of OC film.

View Article and Find Full Text PDF

NysL, a cytochrome P450 monooxygenase from the Gram-positive bacterium Streptomyces noursei, catalyzes the C10 hydroxylation of 10-deoxynystain to nystatin A, a clinically important antifungal. In this study, we present the 2.0 Å resolution crystal structure of NysL bound to nystatin A.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!