Type I beta turns make a new twist in pentapeptide repeat proteins: Crystal structure of Alr5209 from Nostoc sp. PCC 7120 determined at 1.7 angström resolution.

Ruojing Zhang, Shuisong Ni, Michael A Kennedy

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In one paragraph

Article in Journal of structural biology: X. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

0.3field-weighted citation impact, top 44% of its field

1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 3 citations in OpenAlex.

Current Understanding of the Structure and Function of Pentapeptide Repeat Proteins.Biomolecules · 2021
Review

4 · The record

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5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Ruojing ZhangDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, United States.

Shuisong NiDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, United States.

Michael A KennedyDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, United States.

Miami University · US

Funding

Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017

$8.2M

NIGMS NIH HHS P41 GM103311

6 · The paper itself

Abstract

Pentapeptide repeat proteins (PRPs) are found abundantly in cyanobacteria, numbering in the dozens in some genomes, e.g. in Nostoc sp. PCC 7120. PRPs, comprised of a repeating consensus sequence of five amino acids, adopt a distinctive right-handed quadrilateral β-helical structure, also referred to as a repeat five residue (Rfr) fold, made up of stacks of coils formed by four consecutive pentapeptide repeats. The right-handed quadrilateral β-helical PRP structure is constructed by repeating β turns at each of four corners in a given coil, each causing a 90° change in direction of the polypeptide chain. Until now, all PRP structures have consisted either of type II and IV β turns or exclusively of type II β turns. Here, we report the first structure of a PRP comprised of type I and II β turns, Alr5209 from Nostoc sp. PCC 7120. The

Indexed as

Beta turnsCyanobacteriaNostoc sp. PCC 7120Pentapeptide repeat proteinProtein crystal structureRepeat five residue fold

Identifiers

PMID32647815

DOI10.1016/j.yjsbx.2019.100010

PMCPMC7337050

OpenAlexW2968441837

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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.