Structural characterization of metal binding to a cold-adapted frataxin

Verfasser / Beitragende:
[Martín Noguera, Ernesto Roman, Juan Rigal, Alexandra Cousido-Siah, André Mitschler, Alberto Podjarny, Javier Santos]
Ort, Verlag, Jahr:
2015
Enthalten in:
JBIC Journal of Biological Inorganic Chemistry, 20/4(2015-06-01), 653-664
Format:
Artikel (online)
ID: 605507481
LEADER caa a22 4500
001 605507481
003 CHVBK
005 20210128100632.0
007 cr unu---uuuuu
008 210128e20150601xx s 000 0 eng
024 7 0 |a 10.1007/s00775-015-1251-9  |2 doi 
035 |a (NATIONALLICENCE)springer-10.1007/s00775-015-1251-9 
245 0 0 |a Structural characterization of metal binding to a cold-adapted frataxin  |h [Elektronische Daten]  |c [Martín Noguera, Ernesto Roman, Juan Rigal, Alexandra Cousido-Siah, André Mitschler, Alberto Podjarny, Javier Santos] 
520 3 |a Frataxin is an evolutionary conserved protein that participates in iron metabolism. Deficiency of this small protein in humans causes a severe neurodegenerative disease known as Friedreich's ataxia. A number of studies indicate that frataxin binds iron and regulates Fe-S cluster biosynthesis. Previous structural studies showed that metal binding occurs mainly in a region of high density of negative charge. However, a comprehensive characterization of the binding sites is required to gain further insights into the mechanistic details of frataxin function. In this work, we have solved the X-ray crystal structures of a cold-adapted frataxin from a psychrophilic bacterium in the presence of cobalt or europium ions. We have identified a number of metal-binding sites, mainly solvent exposed, several of which had not been observed in previous studies on mesophilic homologues. No major structural changes were detected upon metal binding, although the structures exhibit significant changes in crystallographic B-factors. The analysis of these B-factors, in combination with crystal packing and RMSD among structures, suggests the existence of localized changes in the internal motions. Based on these results, we propose that bacterial frataxins possess binding sites of moderate affinity for a quick capture and transfer of iron to other proteins and for the regulation of Fe-S cluster biosynthesis, modulating interactions with partner proteins. 
540 |a SBIC, 2015 
690 7 |a CyaY protein family  |2 nationallicence 
690 7 |a Iron binding  |2 nationallicence 
690 7 |a X-ray diffraction  |2 nationallicence 
690 7 |a Conformational dynamics  |2 nationallicence 
690 7 |a Extremophile  |2 nationallicence 
700 1 |a Noguera  |D Martín  |u Instituto de Química y Físico-Química Biológicas, Universidad de Buenos Aires, Junín 956, 1113AAD, Buenos Aires, Argentina  |4 aut 
700 1 |a Roman  |D Ernesto  |u Instituto de Química y Físico-Química Biológicas, Universidad de Buenos Aires, Junín 956, 1113AAD, Buenos Aires, Argentina  |4 aut 
700 1 |a Rigal  |D Juan  |u Instituto de Química y Físico-Química Biológicas, Universidad de Buenos Aires, Junín 956, 1113AAD, Buenos Aires, Argentina  |4 aut 
700 1 |a Cousido-Siah  |D Alexandra  |u Department of Integrative Biology, IGBMC, CNRS, INSERM, Université de Strasbourg, Illkirch, France  |4 aut 
700 1 |a Mitschler  |D André  |u Department of Integrative Biology, IGBMC, CNRS, INSERM, Université de Strasbourg, Illkirch, France  |4 aut 
700 1 |a Podjarny  |D Alberto  |u Department of Integrative Biology, IGBMC, CNRS, INSERM, Université de Strasbourg, Illkirch, France  |4 aut 
700 1 |a Santos  |D Javier  |u Instituto de Química y Físico-Química Biológicas, Universidad de Buenos Aires, Junín 956, 1113AAD, Buenos Aires, Argentina  |4 aut 
773 0 |t JBIC Journal of Biological Inorganic Chemistry  |d Springer Berlin Heidelberg  |g 20/4(2015-06-01), 653-664  |x 0949-8257  |q 20:4<653  |1 2015  |2 20  |o 775 
856 4 0 |u https://doi.org/10.1007/s00775-015-1251-9  |q text/html  |z Onlinezugriff via DOI 
898 |a BK010053  |b XK010053  |c XK010000 
900 7 |a Metadata rights reserved  |b Springer special CC-BY-NC licence  |2 nationallicence 
908 |D 1  |a research-article  |2 jats 
949 |B NATIONALLICENCE  |F NATIONALLICENCE  |b NL-springer 
950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1007/s00775-015-1251-9  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Noguera  |D Martín  |u Instituto de Química y Físico-Química Biológicas, Universidad de Buenos Aires, Junín 956, 1113AAD, Buenos Aires, Argentina  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Roman  |D Ernesto  |u Instituto de Química y Físico-Química Biológicas, Universidad de Buenos Aires, Junín 956, 1113AAD, Buenos Aires, Argentina  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Rigal  |D Juan  |u Instituto de Química y Físico-Química Biológicas, Universidad de Buenos Aires, Junín 956, 1113AAD, Buenos Aires, Argentina  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Cousido-Siah  |D Alexandra  |u Department of Integrative Biology, IGBMC, CNRS, INSERM, Université de Strasbourg, Illkirch, France  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Mitschler  |D André  |u Department of Integrative Biology, IGBMC, CNRS, INSERM, Université de Strasbourg, Illkirch, France  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Podjarny  |D Alberto  |u Department of Integrative Biology, IGBMC, CNRS, INSERM, Université de Strasbourg, Illkirch, France  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Santos  |D Javier  |u Instituto de Química y Físico-Química Biológicas, Universidad de Buenos Aires, Junín 956, 1113AAD, Buenos Aires, Argentina  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t JBIC Journal of Biological Inorganic Chemistry  |d Springer Berlin Heidelberg  |g 20/4(2015-06-01), 653-664  |x 0949-8257  |q 20:4<653  |1 2015  |2 20  |o 775