3o55: Difference between revisions
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==Crystal structure of human FAD-linked augmenter of liver regeneration (ALR)== | ==Crystal structure of human FAD-linked augmenter of liver regeneration (ALR)== | ||
<StructureSection load='3o55' size='340' side='right' caption='[[3o55]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='3o55' size='340' side='right'caption='[[3o55]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3o55]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3o55]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O55 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mbg|3mbg]], [[2hj3|2hj3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3mbg|3mbg]], [[2hj3|2hj3]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALR ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3o55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o55 OCA], [https://pdbe.org/3o55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o55 RCSB], [https://www.ebi.ac.uk/pdbsum/3o55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o55 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Banci, L]] | [[Category: Banci, L]] | ||
[[Category: Bertini, I]] | [[Category: Bertini, I]] | ||
Revision as of 10:15, 12 May 2022
Crystal structure of human FAD-linked augmenter of liver regeneration (ALR)Crystal structure of human FAD-linked augmenter of liver regeneration (ALR)
Structural highlights
Publication Abstract from PubMedOxidative protein folding in the mitochondrial intermembrane space requires the transfer of a disulfide bond from MIA40 to the substrate. During this process MIA40 is reduced and regenerated to a functional state through the interaction with the flavin-dependent sulfhydryl oxidase ALR. Here we present the mechanistic basis of ALR-MIA40 interaction at atomic resolution by biochemical and structural analyses of the mitochondrial ALR isoform and its covalent mixed disulfide intermediate with MIA40. This ALR isoform contains a folded FAD-binding domain at the C-terminus and an unstructured, flexible N-terminal domain, weakly and transiently interacting one with the other. A specific region of the N-terminal domain guides the interaction with the MIA40 substrate binding cleft (mimicking the interaction of the substrate itself), without being involved in the import of ALR. The hydrophobicity-driven binding of this region ensures precise protein-protein recognition needed for an efficient electron transfer process. Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR.,Banci L, Bertini I, Calderone V, Cefaro C, Ciofi-Baffoni S, Gallo A, Kallergi E, Lionaki E, Pozidis C, Tokatlidis K Proc Natl Acad Sci U S A. 2011 Mar 22;108(12):4811-6. Epub 2011 Mar 7. PMID:21383138[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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