7tfm: Difference between revisions

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'''Unreleased structure'''


The entry 7tfm is ON HOLD
==Atomic Structure of the Leishmania spp. Hsp100 N-Domain==
<StructureSection load='7tfm' size='340' side='right'caption='[[7tfm]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7tfm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_mexicana_MHOM/GT/2001/U1103 Leishmania mexicana MHOM/GT/2001/U1103]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TFM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.055&#8491;</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></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=7tfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tfm OCA], [https://pdbe.org/7tfm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tfm RCSB], [https://www.ebi.ac.uk/pdbsum/7tfm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tfm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E9ALU6_LEIMU E9ALU6_LEIMU]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hsp100 is an ATP-dependent unfoldase that promotes protein disaggregation or facilitates the unfolding of aggregation-prone polypeptides marked for degradation. Recently, new Hsp100 functions are emerging. In Plasmodium, an Hsp100 drives malaria protein export, presenting a novel drug target. Whether Hsp100 has a similar function in other protists is unknown. We present the 1.06-A resolution crystal structure of the Hsp100 N-domain from Leishmania spp., the causative agent of leishmaniasis in humans. Our structure reveals a network of methionines and aromatic amino acids that define the putative substrate-binding site and likely evolved to protect Hsp100 from oxidative damage in host immune cells.


Authors:  
Atomic Structure of the Leishmania spp. Hsp100 N-Domain.,Mercado JM, Lee S, Chang C, Sung N, Soong L, Catic A, Tsai FTF Proteins. 2022 Feb 4. doi: 10.1002/prot.26310. PMID:35122310<ref>PMID:35122310</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 7tfm" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Leishmania mexicana MHOM/GT/2001/U1103]]
[[Category: Catic A]]
[[Category: Chang C]]
[[Category: Lee S]]
[[Category: Mercado JM]]
[[Category: Soong L]]
[[Category: Sung N]]
[[Category: Tsai FTF]]
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