8eky: Difference between revisions
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==Cryo-EM structure of the human PRDX4-ErP46 complex== | |||
<StructureSection load='8eky' size='340' side='right'caption='[[8eky]], [[Resolution|resolution]] 3.47Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8eky]] is a 11 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=8EKY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EKY FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.47Å</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=8eky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8eky OCA], [https://pdbe.org/8eky PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8eky RCSB], [https://www.ebi.ac.uk/pdbsum/8eky PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8eky ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PRDX4_HUMAN PRDX4_HUMAN] Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.<ref>PMID:9388242</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We applied raw human liver microsome lysate to a holey carbon grid and used cryo-electron microscopy (cryo-EM) to define its composition. From this sample we identified and simultaneously determined high-resolution structural information for ten unique human liver enzymes involved in diverse cellular processes. Notably, we determined the structure of the endoplasmic bifunctional protein H6PD, where the N- and C-terminal domains independently possess glucose-6-phosphate dehydrogenase and 6-phosphogluconolactonase enzymatic activity, respectively. We also obtained the structure of heterodimeric human GANAB, an ER glycoprotein quality-control machinery that contains a catalytic alpha subunit and a noncatalytic beta subunit. In addition, we observed a decameric peroxidase, PRDX4, which directly contacts a disulfide isomerase-related protein, ERp46. Structural data suggest that several glycosylations, bound endogenous compounds, and ions associate with these human liver enzymes. These results highlight the importance of cryo-EM in facilitating the elucidation of human organ proteomics at the atomic level. | |||
High-resolution structural-omics of human liver enzymes.,Su CC, Lyu M, Zhang Z, Miyagi M, Huang W, Taylor DJ, Yu EW Cell Rep. 2023 Jun 27;42(6):112609. doi: 10.1016/j.celrep.2023.112609. Epub 2023 , Jun 7. PMID:37289586<ref>PMID:37289586</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Su | <div class="pdbe-citations 8eky" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Su CC]] | |||
Latest revision as of 14:31, 6 November 2024
Cryo-EM structure of the human PRDX4-ErP46 complex
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