7us2: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: '''Unreleased structure''' The entry 7us2 is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures
 
No edit summary
 
(2 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 7us2 is ON HOLD  until Paper Publication
==PARL-cleaved Skd3 (human ClpB) E455Q Nucleotide Binding Domain hexamer bound to ATPgammaS, open conformation==
 
<StructureSection load='7us2' size='340' side='right'caption='[[7us2]], [[Resolution|resolution]] 2.76&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[7us2]] is a 7 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=7US2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7US2 FirstGlance]. <br>
Description:  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.76&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=7us2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7us2 OCA], [https://pdbe.org/7us2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7us2 RCSB], [https://www.ebi.ac.uk/pdbsum/7us2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7us2 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/CLPB_HUMAN CLPB_HUMAN] 3-methylglutaconic aciduria type 7;Autosomal dominant severe congenital neutropenia. The disease is caused by variants affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/CLPB_HUMAN CLPB_HUMAN] May function as a regulatory ATPase and be related to secretion/protein trafficking process. Involved in mitochondrial-mediated antiviral innate immunity, activates RIG-I-mediated signal transduction and production of IFNB1 and pro-inflammatory cytokine IL6 (PubMed:31522117).<ref>PMID:31522117</ref>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Cheng Y]]
[[Category: Chio US]]
[[Category: Gupta A]]
[[Category: Lentzsch AM]]
[[Category: Lu C]]
[[Category: Shan S-o]]
[[Category: Siegel AS]]
[[Category: Yu Z]]

Latest revision as of 19:55, 8 November 2023

PARL-cleaved Skd3 (human ClpB) E455Q Nucleotide Binding Domain hexamer bound to ATPgammaS, open conformationPARL-cleaved Skd3 (human ClpB) E455Q Nucleotide Binding Domain hexamer bound to ATPgammaS, open conformation

Structural highlights

7us2 is a 7 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 2.76Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

CLPB_HUMAN 3-methylglutaconic aciduria type 7;Autosomal dominant severe congenital neutropenia. The disease is caused by variants affecting the gene represented in this entry.

Function

CLPB_HUMAN May function as a regulatory ATPase and be related to secretion/protein trafficking process. Involved in mitochondrial-mediated antiviral innate immunity, activates RIG-I-mediated signal transduction and production of IFNB1 and pro-inflammatory cytokine IL6 (PubMed:31522117).[1]

References

  1. Yoshinaka T, Kosako H, Yoshizumi T, Furukawa R, Hirano Y, Kuge O, Tamada T, Koshiba T. Structural Basis of Mitochondrial Scaffolds by Prohibitin Complexes: Insight into a Role of the Coiled-Coil Region. iScience. 2019 Sep 27;19:1065-1078. doi: 10.1016/j.isci.2019.08.056. Epub 2019, Sep 3. PMID:31522117 doi:http://dx.doi.org/10.1016/j.isci.2019.08.056

7us2, resolution 2.76Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA