Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation

Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation

The SRP Alu domain is involved in co-translational protein targeting. Soni et al. investigate the Alu domain of Plasmodium falciparum, the agent of malaria, and find that unlike any other it adopts an open conformation.

Bibliographic Details
Main Authors: Komal Soni, Georg Kempf, Karen Manalastas-Cantos, Astrid Hendricks, Dirk Flemming, Julien Guizetti, Bernd Simon, Friedrich Frischknecht, Dmitri I. Svergun, Klemens Wild, Irmgard Sinning
Format: Article
Language:English
Published: Nature Publishing Group 2021-05-01
Series:Communications Biology
Online Access:https://doi.org/10.1038/s42003-021-02132-y
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spelling doaj-209bda6b89384eceb72f2290525335c32021-05-23T11:28:34ZengNature Publishing GroupCommunications Biology2399-36422021-05-014111410.1038/s42003-021-02132-yStructural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformationKomal Soni0Georg Kempf1Karen Manalastas-Cantos2Astrid Hendricks3Dirk Flemming4Julien Guizetti5Bernd Simon6Friedrich Frischknecht7Dmitri I. Svergun8Klemens Wild9Irmgard Sinning10Heidelberg University Biochemistry Center (BZH)Heidelberg University Biochemistry Center (BZH)European Molecular Biology Laboratory (EMBL)Heidelberg University Biochemistry Center (BZH)Heidelberg University Biochemistry Center (BZH)Integrative Parasitology, Center for Infectious Diseases, Heidelberg University HospitalEuropean Molecular Biology Laboratory (EMBL)Integrative Parasitology, Center for Infectious Diseases, Heidelberg University HospitalEuropean Molecular Biology Laboratory (EMBL)Heidelberg University Biochemistry Center (BZH)Heidelberg University Biochemistry Center (BZH)The SRP Alu domain is involved in co-translational protein targeting. Soni et al. investigate the Alu domain of Plasmodium falciparum, the agent of malaria, and find that unlike any other it adopts an open conformation.https://doi.org/10.1038/s42003-021-02132-y
collection DOAJ
language English
format Article
sources DOAJ
author Komal Soni
Georg Kempf
Karen Manalastas-Cantos
Astrid Hendricks
Dirk Flemming
Julien Guizetti
Bernd Simon
Friedrich Frischknecht
Dmitri I. Svergun
Klemens Wild
Irmgard Sinning
spellingShingle Komal Soni
Georg Kempf
Karen Manalastas-Cantos
Astrid Hendricks
Dirk Flemming
Julien Guizetti
Bernd Simon
Friedrich Frischknecht
Dmitri I. Svergun
Klemens Wild
Irmgard Sinning
Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation
Communications Biology
author_facet Komal Soni
Georg Kempf
Karen Manalastas-Cantos
Astrid Hendricks
Dirk Flemming
Julien Guizetti
Bernd Simon
Friedrich Frischknecht
Dmitri I. Svergun
Klemens Wild
Irmgard Sinning
author_sort Komal Soni
title Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation
title_short Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation
title_full Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation
title_fullStr Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation
title_full_unstemmed Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation
title_sort structural analysis of the srp alu domain from plasmodium falciparum reveals a non-canonical open conformation
publisher Nature Publishing Group
series Communications Biology
issn 2399-3642
publishDate 2021-05-01
description The SRP Alu domain is involved in co-translational protein targeting. Soni et al. investigate the Alu domain of Plasmodium falciparum, the agent of malaria, and find that unlike any other it adopts an open conformation.
url https://doi.org/10.1038/s42003-021-02132-y
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