Object's details: Impact of calcium binding and thionylation of S100A1 protein on its NMR derived structure and backbone dynamics

Provider:Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk

Description

Title:
Impact of calcium binding and thionylation of S100A1 protein on its NMR derived structure and backbone dynamics
Creator:
Nowakowski, Michał;
Ruszczyńska-Bartnik, Katarzyna;
Budzińska, Monika;
Jaremko, Łukasz;
Jaremko, Mariusz;
Zdanowski, Konrad;
Bierzyński, Andrzej;
Ejchart, Andrzej
Description:
S100 proteins play a crucial role in multiple important biological processes in vertebrate organisms acting predominantly as calcium signal transmitters. S100A1 is a typical representative of this family of proteins. Upon binding of four Ca2+ ions it undergoes a dramatic conformational change, resulting in exposure, in each of its two identical subunits, a large hydrophobic cleft that binds to target proteins. It has been shown that abnormal expression of S100A1 is strongly correlated with a number of severe human diseases: cardiomyopathy and neurodegenerative disorders. A few years ago we have found that thionylation of Cys 85 - the unique cysteine in two identical S100A1 subunits – leads to a drastic increase of the protein affinity for calcium. We postulated that the protein activated by thionylation becomes a more efficient calcium signal transmitter. Therefore, we decided to undertake, using NMR methods, a comparative study of structure and dynamics of native and thionylated human S100A1 in its apo and holo states. In this paper we present the results obtained for the both forms of this protein in its holo state and compare them with the previously published structure of native apo S100. The main conclusion that we draw from these results is that the increased calcium binding affinity of S100A1 upon thionylation arises, most probably, from rearrangement of the hydrophobic core in its apo form.
Object availability:
free access
Date:
2013.01.25
Type:
Article;
PeerReviewed
Publisher:
ACS
Relation: http://eprints.ibb.waw.pl/453 ;http://pubs.acs.org/journal/bichaw ;DOI: 10.1021/bi3015407
Subject:
QH301 Biology
Identifier:
Nowakowski, Michał and Ruszczyńska-Bartnik, Katarzyna and Budzińska, Monika and Jaremko, Łukasz and Jaremko, Mariusz and Zdanowski, Konrad and Bierzyński, Andrzej and Ejchart, Andrzej (2013) Impact of calcium binding and thionylation of S100A1 protein on its NMR derived structure and backbone dynamics. Biochemistry, 52 (7). pp. 1149-1159. ISSN Print Edition ISSN: 0006-2960
Data provider:
Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk

Similar objects

Impact of calcium binding and thionylation of S100A1 protein on its NMR derived structure and backbone dynamics

Date:2013.01.25

Type:other

Impact of calcium binding and thionylation of S100A1 protein on its NMR derived structure and backbone dynamics

Date:2013

Type:other

Solution NMR structure and dynamics of human apo-S100A1 protein

Date:2011.05

Type:other

NMR structural studies of the first catalytic half-domain of ubiquitin activating enzyme

Date:2014.01

Type:other

Metal-coupled folding as the driving force for the extreme stability of Rad50 zinc hook dimer assembly

Date:2016.11.03

Type:other

LTR retrotransposons in fungi.

Creator:Muszewska, Anna | Hoffman-Sommer, Marta | Grynberg, Marcin

Date:2011

Type:other

Molecular and Functional Characterization of MobK Protein—A Novel-Type Relaxase Involved in Mobilization for Conjugational Transfer of Klebsiella pneumoniae Plasmid pIGRK

Date:2021

Type:other

Mechanisms of RNA Degradation by the Eukaryotic Exosome

Creator:Tomecki, Rafał | Drążkowska, Karolina | Dziembowski, Andrzej

Date:2010.05.03

Type:other

Federacja Bibliotek Cyfrowych

Object's details: Impact of calcium binding and thionylation of S100A1 protein on its NMR derived structure and backbone dynamics

Description

Similar objects