ArticleJournal of molecular biology2014
Identification of a unique Fe-S cluster binding site in a glycyl-radical type microcompartment shell protein.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- Nature's Anaerobic Toolkit: Glycyl Radical Enzymes and Their Expanding Functional and Mechanistic Diversity.Biochemistry · 2026Review
- Light-Driven Hybrid Nanoreactor Harnessing the Synergy of Carboxysomes and Organic Frameworks for Efficient Hydrogen Production.ACS catalysis · 2024Article
- Recent structural insights into bacterial microcompartment shells.Current opinion in microbiology · 2021Review
- MCPdb: The bacterial microcompartment database.PloS one · 2021Article
- Prokaryotic Organelles: Bacterial Microcompartments inEcoSal Plus · 2020Review
- Exploring Bacterial Microcompartments in the Acetogenic BacteriumFrontiers in microbiology · 2020Article
- Review
- Functionalization of Bacterial Microcompartment Shell Proteins With Covalently Attached Heme.Frontiers in bioengineering and biotechnology · 2019Article
- Bacterial microcompartments.Nature reviews. Microbiology · 2018Review
- Crystal structures of β-carboxysome shell protein CcmP: ligand binding correlates with the closed or open central pore.Journal of experimental botany · 2017Article
- Bioinformatic characterization of glycyl radical enzyme-associated bacterial microcompartments.Applied and environmental microbiology · 2015Article
- Bacterial microcompartments: widespread prokaryotic organelles for isolation and optimization of metabolic pathways.Molecular microbiology · 2015Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Recently, progress has been made toward understanding the functional diversity of bacterial microcompartment (MCP) systems, which serve as protein-based metabolic organelles in diverse microbes. New types of MCPs have been identified, including the glycyl-radical propanediol (Grp) MCP. Within these elaborate protein complexes, BMC-domain shell proteins [bacterial microcompartment (in reference to the shell protein domain)] assemble to form a polyhedral barrier that encapsulates the enzymatic contents of the MCP. Interestingly, the Grp MCP contains a number of shell proteins with unusual sequence features. GrpU is one such shell protein whose amino acid sequence is particularly divergent from other members of the BMC-domain superfamily of proteins that effectively defines all MCPs. Expression, purification, and subsequent characterization of the protein showed, unexpectedly, that it binds an iron-sulfur cluster. We determined X-ray crystal structures of two GrpU orthologs, providing the first structural insight into the homohexameric BMC-domain shell proteins of the Grp system. The X-ray structures of GrpU, both obtained in the apo form, combined with spectroscopic analyses and computational modeling, show that the metal cluster resides in the central pore of the BMC shell protein at a position of broken 6-fold symmetry. The result is a structurally polymorphic iron-sulfur cluster binding site that appears to be unique among metalloproteins studied to date.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.