6xg6
From Proteopedia
(Difference between revisions)
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==Full-length human mitochondrial Hsp90 (TRAP1) with ADP-BeF3== | ==Full-length human mitochondrial Hsp90 (TRAP1) with ADP-BeF3== | ||
- | <StructureSection load='6xg6' size='340' side='right'caption='[[6xg6]]' scene=''> | + | <StructureSection load='6xg6' size='340' side='right'caption='[[6xg6]], [[Resolution|resolution]] 3.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XG6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6XG6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6xg6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_scarlatinae"_klein_1884 "micrococcus scarlatinae" klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XG6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6XG6 FirstGlance]. <br> |
- | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6xg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xg6 OCA], [http://pdbe.org/6xg6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xg6 RCSB], [http://www.ebi.ac.uk/pdbsum/6xg6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xg6 ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fba2, E0F66_06355, GQY31_00620 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1314 "Micrococcus scarlatinae" Klein 1884])</td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6xg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xg6 OCA], [http://pdbe.org/6xg6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xg6 RCSB], [http://www.ebi.ac.uk/pdbsum/6xg6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xg6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/TRAP1_HUMAN TRAP1_HUMAN]] Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, most likely through stabilization of mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA.<ref>PMID:23525905</ref> <ref>PMID:23564345</ref> <ref>PMID:23747254</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Affinity grids have great potential to facilitate rapid preparation of even quite impure samples in single-particle cryo-electron microscopy (EM). Yet despite the promising advances of affinity grids over the past decades, no single strategy has demonstrated general utility. Here we chemically functionalize cryo-EM grids coated with mostly one or two layers of graphene oxide to facilitate affinity capture. The protein of interest is tagged using a system that rapidly forms a highly specific covalent bond to its cognate catcher linked to the grid via a polyethylene glycol (PEG) spacer. Importantly, the spacer keeps particles away from both the air-water interface and the graphene oxide surface, protecting them from potential denaturation and rendering them sufficiently flexible to avoid preferential sample orientation concerns. Furthermore, the PEG spacer successfully reduces nonspecific binding, enabling high-resolution reconstructions from a much cruder lysate sample. | ||
+ | |||
+ | General and robust covalently linked graphene oxide affinity grids for high-resolution cryo-EM.,Wang F, Liu Y, Yu Z, Li S, Feng S, Cheng Y, Agard DA Proc Natl Acad Sci U S A. 2020 Sep 10. pii: 2009707117. doi:, 10.1073/pnas.2009707117. PMID:32913054<ref>PMID:32913054</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6xg6" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Micrococcus scarlatinae klein 1884]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Agard | + | [[Category: Agard, D A]] |
- | [[Category: Liu | + | [[Category: Liu, Y X]] |
- | [[Category: Wang F]] | + | [[Category: Wang, F]] |
+ | [[Category: Chaperone]] | ||
+ | [[Category: Hsp90]] |
Revision as of 06:16, 14 October 2020
Full-length human mitochondrial Hsp90 (TRAP1) with ADP-BeF3
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