A novel trans conformation of ligand-free calmodulin.
Calmodulin (CaM) is a highly conserved eukaryotic protein that binds specifically to more than 100 target proteins in response to calcium (Ca(2+)) signal. CaM adopts a considerable degree of structural plasticity to accomplish this physiological role; however, the nature and extent of this plasticit...
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doaj-806c185c7e2a4cfea05fc0b0fbd553ff2020-11-24T20:40:21ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0181e5483410.1371/journal.pone.0054834A novel trans conformation of ligand-free calmodulin.Veerendra KumarVishnu Priyanka Reddy ChichiliXuhua TangJ SivaramanCalmodulin (CaM) is a highly conserved eukaryotic protein that binds specifically to more than 100 target proteins in response to calcium (Ca(2+)) signal. CaM adopts a considerable degree of structural plasticity to accomplish this physiological role; however, the nature and extent of this plasticity remain to be fully understood. Here, we report the crystal structure of a novel trans conformation of ligand-free CaM where the relative disposition of two lobes of CaM is different, a conformation to-date not reported. While no major structural changes were observed in the independent N- and C-lobes as compared with previously reported structures of Ca(2+)/CaM, the central helix was tilted by ~90° at Arg75. This is the first crystal structure of CaM to show a drastic conformational change in the central helix, and reveals one of several possible conformations of CaM to engage with its binding partner.http://europepmc.org/articles/PMC3558517?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Veerendra Kumar Vishnu Priyanka Reddy Chichili Xuhua Tang J Sivaraman |
spellingShingle |
Veerendra Kumar Vishnu Priyanka Reddy Chichili Xuhua Tang J Sivaraman A novel trans conformation of ligand-free calmodulin. PLoS ONE |
author_facet |
Veerendra Kumar Vishnu Priyanka Reddy Chichili Xuhua Tang J Sivaraman |
author_sort |
Veerendra Kumar |
title |
A novel trans conformation of ligand-free calmodulin. |
title_short |
A novel trans conformation of ligand-free calmodulin. |
title_full |
A novel trans conformation of ligand-free calmodulin. |
title_fullStr |
A novel trans conformation of ligand-free calmodulin. |
title_full_unstemmed |
A novel trans conformation of ligand-free calmodulin. |
title_sort |
novel trans conformation of ligand-free calmodulin. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2013-01-01 |
description |
Calmodulin (CaM) is a highly conserved eukaryotic protein that binds specifically to more than 100 target proteins in response to calcium (Ca(2+)) signal. CaM adopts a considerable degree of structural plasticity to accomplish this physiological role; however, the nature and extent of this plasticity remain to be fully understood. Here, we report the crystal structure of a novel trans conformation of ligand-free CaM where the relative disposition of two lobes of CaM is different, a conformation to-date not reported. While no major structural changes were observed in the independent N- and C-lobes as compared with previously reported structures of Ca(2+)/CaM, the central helix was tilted by ~90° at Arg75. This is the first crystal structure of CaM to show a drastic conformational change in the central helix, and reveals one of several possible conformations of CaM to engage with its binding partner. |
url |
http://europepmc.org/articles/PMC3558517?pdf=render |
work_keys_str_mv |
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