5ieu: Difference between revisions
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New page: '''Unreleased structure''' The entry 5ieu is ON HOLD Authors: Bai, L., Hu, K., Wang, T., Jastrab, J.B., Darwin, K.H., Li, H. Description: Crystal Structure of Mycobacterium Tuberculosi... |
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==Crystal Structure of Mycobacterium Tuberculosis ATP-independent Proteasome Activator Tetramer== | |||
<StructureSection load='5ieu' size='340' side='right'caption='[[5ieu]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ieu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IEU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IEU 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]] 2.8Å</td></tr> | |||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ieu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ieu OCA], [https://pdbe.org/5ieu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ieu RCSB], [https://www.ebi.ac.uk/pdbsum/5ieu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ieu ProSAT]</span></td></tr> | ||
[[Category: | </table> | ||
[[Category: Darwin | == Function == | ||
[[Category: | [https://www.uniprot.org/uniprot/BPA_MYCTU BPA_MYCTU] Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction. Can inhibit degradation of Pup-tagged substrates in vitro by competing with Mpa for association with the proteasome.<ref>PMID:25469515</ref> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycobacterium tuberculosis]] | |||
[[Category: Bai L]] | |||
[[Category: Darwin KH]] | |||
[[Category: Hu K]] | |||
[[Category: Jastrab JB]] | |||
[[Category: Li H]] | |||
[[Category: Wang T]] | |||
Latest revision as of 15:34, 6 March 2024
Crystal Structure of Mycobacterium Tuberculosis ATP-independent Proteasome Activator TetramerCrystal Structure of Mycobacterium Tuberculosis ATP-independent Proteasome Activator Tetramer
Structural highlights
FunctionBPA_MYCTU Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction. Can inhibit degradation of Pup-tagged substrates in vitro by competing with Mpa for association with the proteasome.[1] References
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