4hs5: Difference between revisions
New page: '''Unreleased structure''' The entry 4hs5 is ON HOLD Authors: Roman, E.A., Cousido-siah, A., Mitschler, A., Podjarny, A., Santos, J. Description: Frataxin from Psychromonas ingrahamii ... |
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==Frataxin from Psychromonas ingrahamii as a model to study stability modulation within CyaY protein family== | |||
<StructureSection load='4hs5' size='340' side='right'caption='[[4hs5]], [[Resolution|resolution]] 1.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4hs5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Psychromonas_ingrahamii_37 Psychromonas ingrahamii 37]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HS5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4hs5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hs5 OCA], [https://pdbe.org/4hs5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hs5 RCSB], [https://www.ebi.ac.uk/pdbsum/4hs5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hs5 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CYAY_PSYIN CYAY_PSYIN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Adaptation of life to low temperatures influences both protein stability and flexibility. Thus, proteins from psychrophilic organisms are excellent models to study relations between these properties. Here we focused on frataxin from Psychromonas ingrahamii (pFXN), an extreme psychrophilic sea ice bacterium that can grow at temperatures as low as -12 degrees C. This alpha/beta protein is highly conserved and plays a key role in iron homeostasis as an iron chaperone. In contrast to other frataxin homologs, chemical and temperature unfolding experiments showed that the thermodynamic stability of pFXN is strongly modulated by pHs: ranging from 5.5+/-0.9 (pH6.0) to 0.9+/-0.3kcalmol-1 (pH8.0). This protein was crystallized and its X-ray structure solved at 1.45A. Comparison of B-factor profiles between Escherichia coli and P. ingrahamii frataxin variants (51% of identity) suggests that, although both proteins share the same structural features, their flexibility distribution is different. Molecular dynamics simulations showed that protonation of His44 or His67 in pFXN lowers the mobility of regions encompassing residues 20-30 and the C-terminal end, probably through favorable electrostatic interactions with residues Asp27, Glu42 and Glu99. Since the C-terminal end of the protein is critical for the stabilization of the frataxin fold, the predictions presented may be reporting on the microscopic origin of the decrease in global stability produced near neutral pH in the psychrophilic variant. We propose that suboptimal electrostatic interactions may have been an evolutionary strategy for the adaptation of frataxin flexibility and function to cold environments. | |||
Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family.,Roman EA, Faraj SE, Cousido-Siah A, Mitschler A, Podjarny A, Santos J Biochim Biophys Acta. 2013 Feb 19. pii: S1570-9639(13)00078-2. doi:, 10.1016/j.bbapap.2013.02.015. PMID:23429177<ref>PMID:23429177</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4hs5" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Frataxin 3D Structures|Frataxin 3D Structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Psychromonas ingrahamii 37]] | |||
[[Category: Cousido-siah A]] | |||
[[Category: Mitschler A]] | |||
[[Category: Podjarny A]] | |||
[[Category: Roman EA]] | |||
[[Category: Santos J]] | |||
Latest revision as of 17:10, 8 November 2023
Frataxin from Psychromonas ingrahamii as a model to study stability modulation within CyaY protein familyFrataxin from Psychromonas ingrahamii as a model to study stability modulation within CyaY protein family
Structural highlights
FunctionPublication Abstract from PubMedAdaptation of life to low temperatures influences both protein stability and flexibility. Thus, proteins from psychrophilic organisms are excellent models to study relations between these properties. Here we focused on frataxin from Psychromonas ingrahamii (pFXN), an extreme psychrophilic sea ice bacterium that can grow at temperatures as low as -12 degrees C. This alpha/beta protein is highly conserved and plays a key role in iron homeostasis as an iron chaperone. In contrast to other frataxin homologs, chemical and temperature unfolding experiments showed that the thermodynamic stability of pFXN is strongly modulated by pHs: ranging from 5.5+/-0.9 (pH6.0) to 0.9+/-0.3kcalmol-1 (pH8.0). This protein was crystallized and its X-ray structure solved at 1.45A. Comparison of B-factor profiles between Escherichia coli and P. ingrahamii frataxin variants (51% of identity) suggests that, although both proteins share the same structural features, their flexibility distribution is different. Molecular dynamics simulations showed that protonation of His44 or His67 in pFXN lowers the mobility of regions encompassing residues 20-30 and the C-terminal end, probably through favorable electrostatic interactions with residues Asp27, Glu42 and Glu99. Since the C-terminal end of the protein is critical for the stabilization of the frataxin fold, the predictions presented may be reporting on the microscopic origin of the decrease in global stability produced near neutral pH in the psychrophilic variant. We propose that suboptimal electrostatic interactions may have been an evolutionary strategy for the adaptation of frataxin flexibility and function to cold environments. Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family.,Roman EA, Faraj SE, Cousido-Siah A, Mitschler A, Podjarny A, Santos J Biochim Biophys Acta. 2013 Feb 19. pii: S1570-9639(13)00078-2. doi:, 10.1016/j.bbapap.2013.02.015. PMID:23429177[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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