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3sbz

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<StructureSection load='3sbz' size='340' side='right'caption='[[3sbz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3sbz' size='340' side='right'caption='[[3sbz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3sbz]] 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=3SBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SBZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3sbz]] 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=3SBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SBZ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr>
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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]] 2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3sby|3sby]], [[3sc0|3sc0]]</div></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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MMACHC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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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=3sbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sbz OCA], [https://pdbe.org/3sbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sbz RCSB], [https://www.ebi.ac.uk/pdbsum/3sbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sbz 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=3sbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sbz OCA], [https://pdbe.org/3sbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sbz RCSB], [https://www.ebi.ac.uk/pdbsum/3sbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sbz ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/MMAC_HUMAN MMAC_HUMAN]] Methylmalonic acidemia with homocystinuria, type cblC. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/MMAC_HUMAN MMAC_HUMAN] Methylmalonic acidemia with homocystinuria, type cblC. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/MMAC_HUMAN MMAC_HUMAN]] May be involved in the binding and intracellular trafficking of cobalamin (vitamin B12).
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[https://www.uniprot.org/uniprot/MMAC_HUMAN MMAC_HUMAN] May be involved in the binding and intracellular trafficking of cobalamin (vitamin B12).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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An early step in the intracellular processing of B12 involves CblC, which exhibits dual reactivity, catalyzing the reductive decyanation of cyanocobalamin (vitamin B12) and the dealkylation of alkylcobalamins (e.g. methylcobalamin; MeCbl). Insights into how the CblC scaffold supports this chemical dichotomy have been unavailable despite it being the most common locus of patient mutations associated with inherited cobalamin disorders that manifest in both severe homocystinuria and methylmalonic aciduria. Herein, we report structures of human CblC, with and without bound MeCbl, which provide novel biochemical insights into its mechanism of action. Our results reveal that CblC is the most divergent member of the NADPH-dependent flavin reductase family and can use FMN or FAD as a prosthetic group to catalyze reductive decyanation. Furthermore, CblC is the first example of an enzyme with glutathione transferase activity that has a sequence and structure unrelated to the GST superfamily. CblC thus represents an example of evolutionary adaptation of a common structural platform to perform diverse chemistries. The CblC structure allows us to rationalize the biochemical basis of a number of pathological mutations associated with severe clinical phenotypes.
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The structural basis of multifunctionality in a B12 processing enzyme.,Koutmos M, Gherasim C, Smith JL, Banerjee R J Biol Chem. 2011 Jun 22. PMID:21697092<ref>PMID:21697092</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 3sbz" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Banerjee, R]]
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[[Category: Banerjee R]]
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[[Category: Gherasim, C]]
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[[Category: Gherasim C]]
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[[Category: Koutmos, M]]
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[[Category: Koutmos M]]
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[[Category: Smith, J L]]
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[[Category: Smith JL]]
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[[Category: Cblc]]
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[[Category: Cobalamin]]
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[[Category: Flavin]]
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[[Category: Flavin reductase]]
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[[Category: Glutathione]]
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[[Category: Maturase]]
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[[Category: Mmachc]]
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[[Category: Oxidoreductase]]
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Current revision

Crystal Structure of Apo-MMACHC (1-244), a human B12 processing enzyme

PDB ID 3sbz

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