6mux

From Proteopedia

(Difference between revisions)

Revision as of 02:58, 11 April 2020

The structure of the Plasmodium falciparum 20S proteasome in complex with one PA28 activator

6mux, resolution 3.90Å

Structural highlights

6mux is a 35 chain structure with sequence from Plaf7 and Plasmodium falciparum 3d7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	6dfk, 6muw, 6muv
Gene:	PF3D7_0907700 (PLAF7)
Activity:	Proteasome endopeptidase complex, with EC number 3.4.25.1
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[Q8IKC9_PLAF7] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.[RuleBase:RU004203] [Q8IDG3_PLAF7] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH.[RuleBase:RU000551] [Q8I6T3_PLAF7] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.[RuleBase:RU004203] [Q8IJT1_PLAF7] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.[RuleBase:RU004203] [Q7K6A9_PLAF7] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.[RuleBase:RU004203] [Q8IDG2_PLAF7] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH.[RuleBase:RU000551] [C0H4E8_PLAF7] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.[RuleBase:RU004203] [Q8IBI3_PLAF7] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH.[RuleBase:RU000551]

Publication Abstract from PubMed

The activity of the proteasome 20S catalytic core is regulated by protein complexes that bind to one or both ends. The PA28 regulator stimulates 20S proteasome peptidase activity in vitro, but its role in vivo remains unclear. Here, we show that genetic deletion of the PA28 regulator from Plasmodium falciparum (Pf) renders malaria parasites more sensitive to the antimalarial drug dihydroartemisinin, indicating that PA28 may play a role in protection against proteotoxic stress. The crystal structure of PfPA28 reveals a bell-shaped molecule with an inner pore that has a strong segregation of charges. Small-angle X-ray scattering shows that disordered loops, which are not resolved in the crystal structure, extend from the PfPA28 heptamer and surround the pore. Using single particle cryo-electron microscopy, we solved the structure of Pf20S in complex with one and two regulatory PfPA28 caps at resolutions of 3.9 and 3.8 A, respectively. PfPA28 binds Pf20S asymmetrically, strongly engaging subunits on only one side of the core. PfPA28 undergoes rigid body motions relative to Pf20S. Molecular dynamics simulations support conformational flexibility and a leaky interface. We propose lateral transfer of short peptides through the dynamic interface as a mechanism facilitating the release of proteasome degradation products.

The structure of the PA28-20S proteasome complex from Plasmodium falciparum and implications for proteostasis.,Xie SC, Metcalfe RD, Hanssen E, Yang T, Gillett DL, Leis AP, Morton CJ, Kuiper MJ, Parker MW, Spillman NJ, Wong W, Tsu C, Dick LR, Griffin MDW, Tilley L Nat Microbiol. 2019 Aug 5. pii: 10.1038/s41564-019-0524-4. doi:, 10.1038/s41564-019-0524-4. PMID:31384003^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Xie SC, Metcalfe RD, Hanssen E, Yang T, Gillett DL, Leis AP, Morton CJ, Kuiper MJ, Parker MW, Spillman NJ, Wong W, Tsu C, Dick LR, Griffin MDW, Tilley L. The structure of the PA28-20S proteasome complex from Plasmodium falciparum and implications for proteostasis. Nat Microbiol. 2019 Aug 5. pii: 10.1038/s41564-019-0524-4. doi:, 10.1038/s41564-019-0524-4. PMID:31384003 doi:http://dx.doi.org/10.1038/s41564-019-0524-4

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6mux"

@@ Line 3: / Line 3: @@
 <SX load='6mux' size='340' side='right' viewer='molstar' caption='[[6mux]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6mux]] is a 35 chain structure with sequence from [http://en.wikipedia.org/wiki/Plaf7 Plaf7] and [http://en.wikipedia.org/wiki/Plasmodium_falciparum_3d7 Plasmodium falciparum 3d7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MUX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6mux]] is a 35 chain structure with sequence from [http://en.wikipedia.org/wiki/Plaf7 Plaf7] and [http://en.wikipedia.org/wiki/Plasmodium_falciparum_3d7 Plasmodium falciparum 3d7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MUX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6MUX FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6dfk|6dfk]], [[6muw|6muw]], [[6muv|6muv]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PF3D7_0907700 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6mux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mux OCA], [http://pdbe.org/6mux PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mux RCSB], [http://www.ebi.ac.uk/pdbsum/6mux PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mux ProSAT]</span></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=6mux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mux OCA], [http://pdbe.org/6mux PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mux RCSB], [http://www.ebi.ac.uk/pdbsum/6mux PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mux ProSAT]</span></td></tr>
 </table>
 == Function ==

6mux

From Proteopedia

Revision as of 02:58, 11 April 2020

The structure of the Plasmodium falciparum 20S proteasome in complex with one PA28 activator

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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