3o55

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[[Image:3o55.jpg|left|200px]]
 
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==Crystal structure of human FAD-linked augmenter of liver regeneration (ALR)==
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The line below this paragraph, containing "STRUCTURE_3o55", creates the "Structure Box" on the page.
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<StructureSection load='3o55' size='340' side='right'caption='[[3o55]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<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>
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{{STRUCTURE_3o55| PDB=3o55 | SCENE= }}
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<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>
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</table>
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== Disease ==
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[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.
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Oxidative 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.
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===Crystal structure of human FAD-linked augmenter of liver regeneration (ALR)===
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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<ref>PMID:21383138</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3o55" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 21383138 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_21383138}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[3o55]] is a 1 chain structure with sequence from [http://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].
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==Reference==
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<ref group="xtra">PMID:21383138</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Banci, L.]]
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[[Category: Large Structures]]
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[[Category: Bertini, I.]]
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[[Category: Banci L]]
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[[Category: Calderone, V.]]
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[[Category: Bertini I]]
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[[Category: Cefaro, C.]]
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[[Category: Calderone V]]
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[[Category: Ciofi-Baffoni, S.]]
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[[Category: Cefaro C]]
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[[Category: Gallo, A.]]
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[[Category: Ciofi-Baffoni S]]
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[[Category: Kallergi, E.]]
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[[Category: Gallo A]]
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[[Category: Lionaki, E.]]
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[[Category: Kallergi E]]
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[[Category: Pozidis, C.]]
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[[Category: Lionaki E]]
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[[Category: Tokatlidis, K.]]
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[[Category: Pozidis C]]
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[[Category: Tokatlidis K]]

Current revision

Crystal structure of human FAD-linked augmenter of liver regeneration (ALR)

PDB ID 3o55

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