1q5r

The Rhodococcus 20S proteasome with unprocessed pro-peptidesThe Rhodococcus 20S proteasome with unprocessed pro-peptides

Structural highlights

1q5r is a 14 chain structure with sequence from Rhodococcus erythropolis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.1Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PSB1_RHOER Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The R.erythropolis proteasomes are able to cleave oligopeptides after Tyr, Phe and Leu, very poorly after Arg but not after Glu. Thus, displays chymotrypsin-like activity, low trypsin-like activity but no caspase-like activity.[HAMAP-Rule:MF_02113]^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Tamura T, Nagy I, Lupas A, Lottspeich F, Cejka Z, Schoofs G, Tanaka K, De Mot R, Baumeister W. The first characterization of a eubacterial proteasome: the 20S complex of Rhodococcus. Curr Biol. 1995 Jul 1;5(7):766-74. PMID:7583123
↑ Zuhl F, Tamura T, Dolenc I, Cejka Z, Nagy I, De Mot R, Baumeister W. Subunit topology of the Rhodococcus proteasome. FEBS Lett. 1997 Jan 2;400(1):83-90. PMID:9000518

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OCA

[1] Tamura T, Nagy I, Lupas A, Lottspeich F, Cejka Z, Schoofs G, Tanaka K, De Mot R, Baumeister W. The first characterization of a eubacterial proteasome: the 20S complex of Rhodococcus. Curr Biol. 1995 Jul 1;5(7):766-74. PMID:7583123

[2] Zuhl F, Tamura T, Dolenc I, Cejka Z, Nagy I, De Mot R, Baumeister W. Subunit topology of the Rhodococcus proteasome. FEBS Lett. 1997 Jan 2;400(1):83-90. PMID:9000518

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