Architecture and Evolution of Blade Assembly in beta-propeller
Lectins

J 2019

Architecture and Evolution of Blade Assembly in beta-propeller Lectins

BONNARDEL, Francois, Atul KUMAR, Michaela WIMMEROVÁ, Martina LAHMANN, Serge PEREZ et. al.

Basic information

Original name

Architecture and Evolution of Blade Assembly in beta-propeller Lectins

Authors

BONNARDEL, Francois (250 France), Atul KUMAR (356 India, belonging to the institution), Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution), Martina LAHMANN (752 Sweden), Serge PEREZ (250 France), Annabelle VARROT (250 France), Frederique LISACEK (756 Switzerland) and Anne IMBERTY (250 France)

Edition

Structure, CAMBRIDGE, CELL PRESS, 2019, 0969-2126

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10400 1.4 Chemical sciences

Country of publisher

Switzerland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 4.862

RIV identification code

RIV/00216224:14310/19:00108109

Organization unit

Faculty of Science

DOI

http://dx.doi.org/10.1016/j.str.2019.02.002

UT WoS

000467238900006

Keywords in English

lectin; beta-propellers

Abstract

V originále

Lectins with a beta-propeller fold bind glycans on the cell surface through multivalent binding sites and appropriate directionality. These proteins are formed by repeats of short domains, raising questions about evolutionary duplication. However, these repeats are difficult to detect in translated genomes and seldom correctly annotated in sequence databases. To address these issues, we defined the blade signature of the five types of beta-propellers using 3D-structural data. With these templates, we predicted 3,887 beta-propeller lectins in 1,889 species and organized this information in a searchable online database. The data reveal a widespread distribution of beta-propeller lectins across species. Prediction also emphasizes multiple architectures and led to the discovery of a beta-propeller assembly scenario. This was confirmed by producing and characterizing a predicted protein coded in the genome of Kordia zhangzhouensis. The crystal structure uncovers an intermediate in the evolution of beta-propeller assembly and demonstrates the power of our tools.

Links

GA18-18964S, research and development project

Name: Lektiny a jejich úloha v interakci patogen/hostitel a buněčném rozpoznávání

Investor: Czech Science Foundation

LM2015043, research and development project

Name: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)

Investor: Ministry of Education, Youth and Sports of the CR

LQ1601, research and development project

Name: CEITEC 2020 (Acronym: CEITEC2020)

Investor: Ministry of Education, Youth and Sports of the CR

692068, interní kód MU

Name: BISON - Bridging Structural Biology with Biological Synthesis and Self Assembly to Reveal Key Processes in Living Systems (Acronym: BISON)

Investor: European Union, Spreading excellence and widening participation

90043, large research infrastructures

Name: CIISB

Citovat

BONNARDEL, Francois, Atul KUMAR, Michaela WIMMEROVÁ, Martina LAHMANN, Serge PEREZ, Annabelle VARROT, Frederique LISACEK and Anne IMBERTY. Architecture and Evolution of Blade Assembly in beta-propeller Lectins. Structure. CAMBRIDGE: CELL PRESS, 2019, vol. 27, No 5, p. 764-775. ISSN 0969-2126. Available from: https://dx.doi.org/10.1016/j.str.2019.02.002.

@article{1608896,
   author = {Bonnardel, Francois and Kumar, Atul and Wimmerová, Michaela and Lahmann, Martina and Perez, Serge and Varrot, Annabelle and Lisacek, Frederique and Imberty, Anne},
   article_location = {CAMBRIDGE},
   article_number = {5},
   doi = {http://dx.doi.org/10.1016/j.str.2019.02.002},
   keywords = {lectin; beta-propellers},
   language = {eng},
   issn = {0969-2126},
   journal = {Structure},
   title = {Architecture and Evolution of Blade Assembly in beta-propeller Lectins},
   url = {https://www.sciencedirect.com/science/article/abs/pii/S0969212619300462?via%3Dihub},
   volume = {27},
   year = {2019}
}

TY  - JOUR
ID  - 1608896
AU  - Bonnardel, Francois - Kumar, Atul - Wimmerová, Michaela - Lahmann, Martina - Perez, Serge - Varrot, Annabelle - Lisacek, Frederique - Imberty, Anne
PY  - 2019
TI  - Architecture and Evolution of Blade Assembly in beta-propeller Lectins
JF  - Structure
VL  - 27
IS  - 5
SP  - 764-775
EP  - 764-775
PB  - CELL PRESS
SN  - 09692126
KW  - lectin
KW  - beta-propellers
UR  - https://www.sciencedirect.com/science/article/abs/pii/S0969212619300462?via%3Dihub
L2  - https://www.sciencedirect.com/science/article/abs/pii/S0969212619300462?via%3Dihub
N2  - Lectins with a beta-propeller fold bind glycans on the cell surface through multivalent binding sites and appropriate directionality. These proteins are formed by repeats of short domains, raising questions about evolutionary duplication. However, these repeats are difficult to detect in translated genomes and seldom correctly annotated in sequence databases. To address these issues, we defined the blade signature of the five types of beta-propellers using 3D-structural data. With these templates, we predicted 3,887 beta-propeller lectins in 1,889 species and organized this information in a searchable online database. The data reveal a widespread distribution of beta-propeller lectins across species. Prediction also emphasizes multiple architectures and led to the discovery of a beta-propeller assembly scenario. This was confirmed by producing and characterizing a predicted protein coded in the genome of Kordia zhangzhouensis. The crystal structure uncovers an intermediate in the evolution of beta-propeller assembly and demonstrates the power of our tools.
ER  -

BONNARDEL, Francois, Atul KUMAR, Michaela WIMMEROVÁ, Martina LAHMANN, Serge PEREZ, Annabelle VARROT, Frederique LISACEK and Anne IMBERTY. Architecture and Evolution of Blade Assembly in beta-propeller Lectins. \textit{Structure}. CAMBRIDGE: CELL PRESS, 2019, vol.~27, No~5, p.~764-775. ISSN~0969-2126. Available from: https://dx.doi.org/10.1016/j.str.2019.02.002.

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