3o55: Difference between revisions
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<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 [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3o55]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id=' | <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='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> | <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> | ||
== Disease == | |||
[https://www.uniprot.org/uniprot/ALR_HUMAN ALR_HUMAN] Congenital cataract - progressive muscular hypotonia - hearing loss - developmental delay. The disease is caused by mutations affecting the gene represented in this entry. | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ALR_HUMAN ALR_HUMAN] Isoform 1: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen.<ref>PMID:19397338</ref> <ref>PMID:23186364</ref> <ref>PMID:20593814</ref> <ref>PMID:21383138</ref> <ref>PMID:22224850</ref> Isoform 2: May act as an autocrine hepatotrophic growth factor promoting liver regeneration.<ref>PMID:19397338</ref> <ref>PMID:23186364</ref> <ref>PMID:20593814</ref> <ref>PMID:21383138</ref> <ref>PMID:22224850</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Banci | [[Category: Banci L]] | ||
[[Category: Bertini | [[Category: Bertini I]] | ||
[[Category: Calderone | [[Category: Calderone V]] | ||
[[Category: Cefaro | [[Category: Cefaro C]] | ||
[[Category: Ciofi-Baffoni | [[Category: Ciofi-Baffoni S]] | ||
[[Category: Gallo | [[Category: Gallo A]] | ||
[[Category: Kallergi | [[Category: Kallergi E]] | ||
[[Category: Lionaki | [[Category: Lionaki E]] | ||
[[Category: Pozidis | [[Category: Pozidis C]] | ||
[[Category: Tokatlidis | [[Category: Tokatlidis K]] | ||
Latest revision as of 12:27, 6 September 2023
Crystal structure of human FAD-linked augmenter of liver regeneration (ALR)Crystal structure of human FAD-linked augmenter of liver regeneration (ALR)
Structural highlights
DiseaseALR_HUMAN Congenital cataract - progressive muscular hypotonia - hearing loss - developmental delay. The disease is caused by mutations affecting the gene represented in this entry. FunctionALR_HUMAN Isoform 1: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen.[1] [2] [3] [4] [5] Isoform 2: May act as an autocrine hepatotrophic growth factor promoting liver regeneration.[6] [7] [8] [9] [10] 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[11] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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