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<StructureSection load='3m9h' size='340' side='right'caption='[[3m9h]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3m9h' size='340' side='right'caption='[[3m9h]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3m9h]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M9H FirstGlance]. <br>
<table><tr><td colspan='2'>[[3m9h]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M9H FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3m91|3m91]], [[3m9b|3m9b]], [[3m9d|3m9d]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mpa ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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=3m9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m9h OCA], [https://pdbe.org/3m9h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m9h RCSB], [https://www.ebi.ac.uk/pdbsum/3m9h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m9h ProSAT]</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=3m9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m9h OCA], [https://pdbe.org/3m9h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m9h RCSB], [https://www.ebi.ac.uk/pdbsum/3m9h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m9h ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/ARC_MYCTU ARC_MYCTU] ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Is required but not sufficient to confer resistance against the lethal effects of reactive nitrogen intermediates (RNI), antimicrobial molecules produced by activated macrophages and other cell types.[HAMAP-Rule:MF_02112]<ref>PMID:14671303</ref> <ref>PMID:15659170</ref> <ref>PMID:17082771</ref> <ref>PMID:19836337</ref> <ref>PMID:20203624</ref>  
Mycobacterium tuberculosis uses a proteasome system that is analogous to the eukaryotic ubiquitin-proteasome pathway and is required for pathogenesis. However, the bacterial analog of ubiquitin, prokaryotic ubiquitin-like protein (Pup), is an intrinsically disordered protein that bears little sequence or structural resemblance to the highly structured ubiquitin. Thus, it was unknown how pupylated proteins were recruited to the proteasome. Here, we show that the Mycobacterium proteasomal ATPase (Mpa) has three pairs of tentacle-like coiled coils that recognize Pup. Mpa bound unstructured Pup through hydrophobic interactions and a network of hydrogen bonds, leading to the formation of an alpha-helix in Pup. Our work describes a binding-induced folding recognition mechanism in the Pup-proteasome system that differs mechanistically from substrate recognition in the ubiquitin-proteasome system. This key difference between the prokaryotic and eukaryotic systems could be exploited for the development of a small molecule-based treatment for tuberculosis.
 
Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation.,Wang T, Darwin KH, Li H Nat Struct Mol Biol. 2010 Oct 17. PMID:20953180<ref>PMID:20953180</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3m9h" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Myctu]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Li, H]]
[[Category: Li H]]
[[Category: Wang, T]]
[[Category: Wang T]]
[[Category: Atp-binding]]
[[Category: Chaperone]]
[[Category: Four helix antiparallel bundle]]
[[Category: Nucleotide-binding]]
[[Category: Proteasome]]
[[Category: S-nitrosylation]]
[[Category: Virulence]]

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