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Structure of angiogenin dimer bound to double-stranded RNA

Angiogenin is an unusual member of the RNase A family and is of great interest in multiple pathological contexts. Although it has been assigned various regulatory roles, its core catalytic function is that of an RNA endonuclease. However, its catalytic efficiency is comparatively low and this has be...

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Autores principales: Sievers, Katharina, Ficner, Ralf
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9435672/
https://www.ncbi.nlm.nih.gov/pubmed/36048083
http://dx.doi.org/10.1107/S2053230X22008317
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author Sievers, Katharina
Ficner, Ralf
author_facet Sievers, Katharina
Ficner, Ralf
author_sort Sievers, Katharina
collection PubMed
description Angiogenin is an unusual member of the RNase A family and is of great interest in multiple pathological contexts. Although it has been assigned various regulatory roles, its core catalytic function is that of an RNA endonuclease. However, its catalytic efficiency is comparatively low and this has been linked to a unique C-terminal helix which partially blocks its RNA-binding site. Assuming that binding to its RNA substrate could trigger a conformational rearrangement, much speculation has arisen on the topic of the interaction of angiogenin with RNA. To date, no structural data on angiogenin–RNA interactions have been available. Here, the structure of angiogenin bound to a double-stranded RNA duplex is reported. The RNA does not reach the active site of angiogenin and no structural arrangement of the C-terminal domain is observed. However, angiogenin forms a previously unobserved crystallographic dimer that makes several backbone interactions with the major and minor grooves of the RNA double helix.
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spelling pubmed-94356722022-10-03 Structure of angiogenin dimer bound to double-stranded RNA Sievers, Katharina Ficner, Ralf Acta Crystallogr F Struct Biol Commun Research Communications Angiogenin is an unusual member of the RNase A family and is of great interest in multiple pathological contexts. Although it has been assigned various regulatory roles, its core catalytic function is that of an RNA endonuclease. However, its catalytic efficiency is comparatively low and this has been linked to a unique C-terminal helix which partially blocks its RNA-binding site. Assuming that binding to its RNA substrate could trigger a conformational rearrangement, much speculation has arisen on the topic of the interaction of angiogenin with RNA. To date, no structural data on angiogenin–RNA interactions have been available. Here, the structure of angiogenin bound to a double-stranded RNA duplex is reported. The RNA does not reach the active site of angiogenin and no structural arrangement of the C-terminal domain is observed. However, angiogenin forms a previously unobserved crystallographic dimer that makes several backbone interactions with the major and minor grooves of the RNA double helix. International Union of Crystallography 2022-08-30 /pmc/articles/PMC9435672/ /pubmed/36048083 http://dx.doi.org/10.1107/S2053230X22008317 Text en © Sievers and Ficner 2022 https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Research Communications
Sievers, Katharina
Ficner, Ralf
Structure of angiogenin dimer bound to double-stranded RNA
title Structure of angiogenin dimer bound to double-stranded RNA
title_full Structure of angiogenin dimer bound to double-stranded RNA
title_fullStr Structure of angiogenin dimer bound to double-stranded RNA
title_full_unstemmed Structure of angiogenin dimer bound to double-stranded RNA
title_short Structure of angiogenin dimer bound to double-stranded RNA
title_sort structure of angiogenin dimer bound to double-stranded rna
topic Research Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9435672/
https://www.ncbi.nlm.nih.gov/pubmed/36048083
http://dx.doi.org/10.1107/S2053230X22008317
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