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| | <StructureSection load='4lk8' size='340' side='right'caption='[[4lk8]], [[Resolution|resolution]] 1.49Å' scene=''> | | <StructureSection load='4lk8' size='340' side='right'caption='[[4lk8]], [[Resolution|resolution]] 1.49Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4lk8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Psyin Psyin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LK8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4lk8]] 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=4LK8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LK8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hs5|4hs5]]</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=4lk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lk8 OCA], [https://pdbe.org/4lk8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lk8 RCSB], [https://www.ebi.ac.uk/pdbsum/4lk8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lk8 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cyaY, Ping_0042 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=357804 PSYIN])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lk8 OCA], [http://pdbe.org/4lk8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lk8 RCSB], [http://www.ebi.ac.uk/pdbsum/4lk8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lk8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CYAY_PSYIN CYAY_PSYIN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Frataxin|Frataxin]] | + | *[[Frataxin 3D Structures|Frataxin 3D Structures]] |
| - | *[[Journal:JBIC:30|Journal:JBIC:30]]
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Psyin]] | + | [[Category: Psychromonas ingrahamii 37]] |
| - | [[Category: Cousido-Siah, A]] | + | [[Category: Cousido-Siah A]] |
| - | [[Category: Mitschler, A]] | + | [[Category: Mitschler A]] |
| - | [[Category: Noguera, M E]] | + | [[Category: Noguera ME]] |
| - | [[Category: Podjarny, A]] | + | [[Category: Podjarny A]] |
| - | [[Category: Roman, E A]] | + | [[Category: Roman EA]] |
| - | [[Category: Santos, J]] | + | [[Category: Santos J]] |
| - | [[Category: Metal binding protein]]
| + | |
| Structural highlights
Function
CYAY_PSYIN
Publication Abstract from PubMed
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.
Structural characterization of metal binding to a cold-adapted frataxin.,Noguera ME, Roman EA, Rigal JB, Cousido-Siah A, Mitschler A, Podjarny A, Santos J J Biol Inorg Chem. 2015 Apr 2. PMID:25832196[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Noguera ME, Roman EA, Rigal JB, Cousido-Siah A, Mitschler A, Podjarny A, Santos J. Structural characterization of metal binding to a cold-adapted frataxin. J Biol Inorg Chem. 2015 Apr 2. PMID:25832196 doi:http://dx.doi.org/10.1007/s00775-015-1251-9
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