Protein Structures Forming the Shell of Primitive Bacterial Organelles
@article{Kerfeld2005ProteinSF, title={Protein Structures Forming the Shell of Primitive Bacterial Organelles}, author={Cheryl A. Kerfeld and Michael R. Sawaya and Shiho Tanaka and C. V. Nguyen and Martin L. Phillips and Morgan Beeby and Todd O. Yeates}, journal={Science}, year={2005}, volume={309}, pages={936 - 938} }
Bacterial microcompartments are primitive organelles composed entirely of protein subunits. Genomic sequence databases reveal the widespread occurrence of microcompartments across diverse microbes. The prototypical bacterial microcompartment is the carboxysome, a protein shell for sequestering carbon fixation reactions. We report three-dimensional crystal structures of multiple carboxysome shell proteins, revealing a hexameric unit as the basic microcompartment building block and showing how…
416 Citations
Recent structural insights into bacterial microcompartment shells.
- BiologyCurrent opinion in microbiology
- 2021
The Shells of BMC-Type Microcompartment Organelles in Bacteria
- BiologyJournal of Molecular Microbiology and Biotechnology
- 2013
This review updates the understanding of bacterial microcompartment shells, how they are assembled, and how they carry out their functions in molecular transport and enzyme organization.
Bacterial microcompartment organelles: protein shell structure and evolution.
- Biology, EngineeringAnnual review of biophysics
- 2010
Current structural, evolutionary, and mechanistic ideas are discussed, along with genomic studies for exploring the function and diversity of this family of bacterial organelles.
Structural characterization of hexameric shell proteins from two types of choline-utilization bacterial microcompartments.
- Biology, ChemistryActa crystallographica. Section F, Structural biology communications
- 2021
Six structures of hexameric shell proteins from type I and type II choline-utilization microcompartments are reported, revealing electrostatic surface properties that are shared between the four types of shell proteins described here.
Atomic-Level Models of the Bacterial Carboxysome Shell
- ChemistryScience
- 2008
Two proteins of previously unknown function assemble to form pentameric structures whose size and shape are compatible with formation of vertices in an icosahedral shell, and combining these pentamers with the hexamers previously elucidated gives two plausible, preliminary atomic models for the carboxysome shell.
Protein-based organelles in bacteria: carboxysomes and related microcompartments
- Biology, Environmental ScienceNature Reviews Microbiology
- 2008
The carboxysome, a prototypical bacterial microcompartment that is found in cyanobacteria and some chemoautotrophs, encapsulates ribulose-1,5-bisphosphate carboxylase/oxygenase and carbonic anhydrase, and thereby enhances carbon fixation by elevating the levels of CO2 in the vicinity of RuBisCO.
Assembly principles and structure of a 6.5-MDa bacterial microcompartment shell
- BiologyScience
- 2017
The crystal structure of an intact shell from Haliangium ochraceum is presented, revealing the basic principles of bacterial microcompartment shell construction and can inform the design and engineering of shells with new functionalities.
Bacterial microcompartments insights into the structure, mechanism, and engineering applications.
- BiologyProgress in molecular biology and translational science
- 2011
Bacterial microcompartments moving into a synthetic biological world.
- Biology, EngineeringJournal of biotechnology
- 2013
References
SHOWING 1-10 OF 29 REFERENCES
Microcompartments in Prokaryotes: Carboxysomes and Related Polyhedra
- BiologyApplied and Environmental Microbiology
- 2001
This review evaluates the evidence that relates carboxysome structure to function in the carbon metabolism of autotrophic prokaryotes and examines similarities to newly discovered particles found in heterotrophs.
A HEX-1 crystal lattice required for Woronin body function in Neurospora crassa
- BiologyNature Structural Biology
- 2003
The crystal structure of HEX-1 is solved at 1.8 Å, which provides the structural basis of its self-assembly and reveals the existence of three intermolecular interfaces that promote the formation of a three-dimensional protein lattice.
THE CARBOXYSOMES (POLYHEDRAL BODIES) OF AUTOTROPHIC PROKARYGTES
- Environmental Science, Biology
- 1984
1. Polyhedral bodies are present in several groups of autotrophic bacteria that assimilate inorganic carbon via the Calvin cycle, including members of the colourless sulphur‐ oxidizing bacteria,…
Minor proteins, mobile arms and membrane–capsid interactions in the bacteriophage PRD1 capsid
- Biology, ChemistryNature Structural Biology
- 2002
Multiresolution models of the PRD1 capsid provide fine details of the molecular interactions associated with particle stability and membrane dynamics and newly revealed proteins suggest how the metastable vertex works and how the capsid edges are stabilized.
The carboxysome, a prokaryotic organelle: a mini-review
- Biology, Chemistry
- 1991
The structure, composition, and function of carboxysomes are studied with great interest and ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is demonstrated to be associated with these prokaryotic inclusions.
L-A virus at 3.4 Å resolution reveals particle architecture and mRNA decapping mechanism
- ChemistryNature Structural Biology
- 2002
The structure of the yeast L-A virus is determined by X-ray crystallography and reveals a trench at the active site of the decapping reaction and suggests a role for nearby residues in the reaction.
The complete atomic structure of the large ribosomal subunit at 2.4 A resolution.
- ChemistryScience
- 2000
The crystal structure of the large ribosomal subunit from Haloarcula marismortui is determined at 2.4 angstrom resolution, and it includes 2833 of the subunit's 3045 nucleotides and 27 of its 31 proteins.
A Novel Evolutionary Lineage of Carbonic Anhydrase (ε Class) Is a Component of the Carboxysome Shell
- Biology, Environmental ScienceJournal of bacteriology
- 2004
It is reported that the carboxysomal shell protein, CsoS3, from Halothiobacillus neapolitanus is a novel carbonic anhydrase (epsilon-class CA) that has an evolutionary lineage distinct from those previously recognized in animals, plants, and other prokaryotes.
Translocation portals for the substrates and products of a viral transcription complex: the bluetongue virus core
- BiologyThe EMBO journal
- 2001
To determine how the logistical problems of transcription within a sealed shell are solved, core crystals were soaked with various ligands and analysed by X‐ray crystallography, demonstrating that nucleotides also bind to the outer core layer, providing a substrate sink.
Functional Organelles in Prokaryotes: Polyhedral Inclusions (Carboxysomes) of Thiobacillus neapolitanus
- BiologyScience
- 1973
The polyhedral inclusions of Thiobacillus neapolitanus have been isolated; they contain ribulose diphosphate carboxylase.