5gjr

From Proteopedia

(Difference between revisions)

Current revision

An atomic structure of the human 26S proteasome

5gjr, resolution 3.50Å

Structural highlights

5gjr is a 20 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 3.5Å
Ligands:
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PSB5_HUMAN 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. This unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib. May catalyze basal processing of intracellular antigens. Plays a role in the protection against oxidative damage through the Nrf2-ARE pathway (By similarity).

Publication Abstract from PubMed

We report the cryo-EM structure of the human 26S proteasome at an average resolution of 3.5 A, allowing atomic modeling of 28 subunits in the core particle (CP) and 18 subunits in the regulatory particle (RP). The C-terminal residues of Rpt3 and Rpt5 subunits in the RP can be seen inserted into surface pockets formed between adjacent alpha subunits in the CP. Each of the six Rpt subunits contains a bound nucleotide, and the central gate of the CP alpha-ring is closed despite RP association. The six pore 1 loops in the Rpt ring are arranged similarly to a spiral staircase along the axial channel of substrate transport, which is constricted by the pore 2 loops. We also determined the cryo-EM structure of the human proteasome bound to the deubiquitinating enzyme USP14 at 4.35-A resolution. Together, our structures provide a framework for mechanistic understanding of eukaryotic proteasome function.

An atomic structure of the human 26S proteasome.,Huang X, Luan B, Wu J, Shi Y Nat Struct Mol Biol. 2016 Jul 18. doi: 10.1038/nsmb.3273. PMID:27428775^[1]

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

References

↑ Huang X, Luan B, Wu J, Shi Y. An atomic structure of the human 26S proteasome. Nat Struct Mol Biol. 2016 Jul 18. doi: 10.1038/nsmb.3273. PMID:27428775 doi:http://dx.doi.org/10.1038/nsmb.3273

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/5gjr"

@@ Line 9: / Line 9: @@
 </table>
 == Function ==
-[https://www.uniprot.org/uniprot/PRS4_HUMAN PRS4_HUMAN] The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.
+[https://www.uniprot.org/uniprot/PSB5_HUMAN PSB5_HUMAN] 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. This unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib. May catalyze basal processing of intracellular antigens. Plays a role in the protection against oxidative damage through the Nrf2-ARE pathway (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

5gjr

From Proteopedia

Current revision

An atomic structure of the human 26S proteasome

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox