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Current Understanding of the Structure and Function of Pentapeptide Repeat Proteins

Department of Chemistry and Biochemistry, 106 Hughes Laboratories, Miami University, Oxford, OH 45056, USA
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Author to whom correspondence should be addressed.
Academic Editor: Vladimir N. Uversky
Biomolecules 2021, 11(5), 638; https://doi.org/10.3390/biom11050638
Received: 29 March 2021 / Revised: 13 April 2021 / Accepted: 17 April 2021 / Published: 26 April 2021
The pentapeptide repeat protein (PRP) superfamily, identified in 1998, has grown to nearly 39,000 sequences from over 3300 species. PRPs, recognized as having at least eight contiguous pentapeptide repeats (PRs) of a consensus pentapeptide sequence, adopt a remarkable structure, namely, a right-handed quadrilateral β-helix with four consecutive PRs forming a single β-helix coil. Adjacent coils join together to form a β-helix “tower” stabilized by β-ladders on the tower faces and type I, type II, or type IV β-turns facilitating an approximately −90° redirection of the polypeptide chain joining one coil face to the next. PRPs have been found in all branches of life, but they are predominantly found in cyanobacteria. Cyanobacteria have existed on earth for more than two billion years and are thought to be responsible for oxygenation of the earth’s atmosphere. Filamentous cyanobacteria such as Nostoc sp. strain PCC 7120 may also represent the oldest and simplest multicellular organisms known to undergo cell differentiation on earth. Knowledge of the biochemical function of these PRPs is essential to understanding how ancient cyanobacteria achieved functions critical to early development of life on earth. PRPs are predicted to exist in all cyanobacteria compartments including thylakoid and cell-wall membranes, cytoplasm, and thylakoid periplasmic space. Despite their intriguing structure and importance to understanding ancient cyanobacteria, the biochemical functions of PRPs in cyanobacteria remain almost completely unknown. The precise biochemical function of only a handful of PRPs is currently known from any organisms, and three-dimensional structures of only sixteen PRPs or PRP-containing multidomain proteins from any organism have been reported. In this review, the current knowledge of the structures and functions of PRPs is presented and discussed. View Full-Text
Keywords: cyanobacteria; filamentous cyanobacteria; heterocyst; Nostoc sp. strain Pcc7120; pentapeptide repeat protein; protein crystallography; repeat five residue fold cyanobacteria; filamentous cyanobacteria; heterocyst; Nostoc sp. strain Pcc7120; pentapeptide repeat protein; protein crystallography; repeat five residue fold
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MDPI and ACS Style

Zhang, R.; Kennedy, M.A. Current Understanding of the Structure and Function of Pentapeptide Repeat Proteins. Biomolecules 2021, 11, 638. https://doi.org/10.3390/biom11050638

AMA Style

Zhang R, Kennedy MA. Current Understanding of the Structure and Function of Pentapeptide Repeat Proteins. Biomolecules. 2021; 11(5):638. https://doi.org/10.3390/biom11050638

Chicago/Turabian Style

Zhang, Ruojing; Kennedy, Michael A. 2021. "Current Understanding of the Structure and Function of Pentapeptide Repeat Proteins" Biomolecules 11, no. 5: 638. https://doi.org/10.3390/biom11050638

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