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7p8w
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7p8w is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Human erythrocyte catalase cryoEM== | |
| + | <StructureSection load='7p8w' size='340' side='right'caption='[[7p8w]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7p8w]] is a 4 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=7P8W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P8W FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CAT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Catalase Catalase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </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=7p8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p8w OCA], [https://pdbe.org/7p8w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p8w RCSB], [https://www.ebi.ac.uk/pdbsum/7p8w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p8w ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[https://www.uniprot.org/uniprot/CATA_HUMAN CATA_HUMAN]] Defects in CAT are the cause of acatalasemia (ACATLAS) [MIM:[https://omim.org/entry/614097 614097]]. A metabolic disorder characterized by absence of catalase activity in red cells and is often associated with ulcerating oral lesions.<ref>PMID:2308162</ref> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/CATA_HUMAN CATA_HUMAN]] Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells.<ref>PMID:7882369</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | One of the key goals in single-particle cryo-microscopy is to obtain a uniform distribution of particle orientations, so that the three-dimensional structure has isotropic resolution in Fourier space. A common problem arises from the interaction of protein molecules with the air-water interface that exists on both surfaces of the thin film of liquid that is formed prior to plunge-freezing into liquid ethane. Some proteins and other macromolecular complexes are disrupted by interaction with the air-water interface. Other proteins or macromolecules either become concentrated through their interaction with the interface or are excluded because they bind strongly to some other part of the grid or the filter paper used in blotting. In this paper, the interaction of human erythrocyte catalase with the air-water interface is investigated and minimized by the addition of certain detergents. Detergents can form an amphipathic monolayer at the air-water interface that creates a barrier and leaves the molecules free to adopt a variety of orientations, thus facilitating the 3D structure determination. These results suggest that further characterization and development of detergents for cryo-microscopy plunge-freezing would be useful. | ||
| - | + | Interaction of human erythrocyte catalase with air-water interface in cryoEM.,Chen S, Li J, Vinothkumar KR, Henderson R Microscopy (Oxf). 2022 Feb 18;71(Supplement_1):i51-i59. doi:, 10.1093/jmicro/dfab037. PMID:35275189<ref>PMID:35275189</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7p8w" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Catalase]] | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chen, S]] | ||
| + | [[Category: Henderson, R]] | ||
| + | [[Category: Li, J]] | ||
| + | [[Category: Vinothkumar, K R]] | ||
| + | [[Category: Human erythrocyte catalase cryoem]] | ||
| + | [[Category: Oxidoreductase]] | ||
Current revision
Human erythrocyte catalase cryoEM
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