This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

6bdf

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 10:18, 1 January 2020

2.8 A resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy

Structural highlights

6bdf is a 28 chain structure with sequence from "thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	psmA, Ta1288 ("Thermoplasma acidophila" (sic) Darland et al. 1970), psmB, Ta0612 ("Thermoplasma acidophila" (sic) Darland et al. 1970)
Activity:	Proteasome endopeptidase complex, with EC number 3.4.25.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PSA_THEAC] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities.^[1] [PSB_THEAC] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities.^[2]

Publication Abstract from PubMed

Recent developments in detector hardware and image-processing software have revolutionized single particle cryo-electron microscopy (cryoEM) and led to a wave of near-atomic resolution (typically approximately 3.3 A) reconstructions. Reaching resolutions higher than 3 A is a prerequisite for structure-based drug design and for cryoEM to become widely interesting to pharmaceutical industries. We report here the structure of the 700 kDa Thermoplasma acidophilum 20S proteasome (T20S), determined at 2.8 A resolution by single-particle cryoEM. The quality of the reconstruction enables identifying the rotameric conformation adopted by some amino-acid side chains (rotamers) and resolving ordered water molecules, in agreement with the expectations for crystal structures at similar resolutions. The results described in this manuscript demonstrate that single particle cryoEM is capable of competing with X-ray crystallography for determination of protein structures of suitable quality for rational drug design.

2.8 A resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy.,Campbell MG, Veesler D, Cheng A, Potter CS, Carragher B Elife. 2015 Mar 11;4. doi: 10.7554/eLife.06380. PMID:25760083^[3]

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

References

↑ Akopian TN, Kisselev AF, Goldberg AL. Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum. J Biol Chem. 1997 Jan 17;272(3):1791-8. PMID:8999862
↑ Akopian TN, Kisselev AF, Goldberg AL. Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum. J Biol Chem. 1997 Jan 17;272(3):1791-8. PMID:8999862
↑ Campbell MG, Veesler D, Cheng A, Potter CS, Carragher B. 2.8 A resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy. Elife. 2015 Mar 11;4. doi: 10.7554/eLife.06380. PMID:25760083 doi:http://dx.doi.org/10.7554/eLife.06380

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/6bdf"

@@ Line 1: / Line 1: @@
 ==2.8 A resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy==
-<StructureSection load='6bdf' size='340' side='right' caption='[[6bdf]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+<StructureSection load='6bdf' size='340' side='right'caption='[[6bdf]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[6bdf]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BDF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BDF FirstGlance]. <br>
@@ Line 21: / Line 21: @@
 ==See Also==
-*[[Proteasome|Proteasome]]
+*[[Proteasome 3D structures|Proteasome 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Proteasome endopeptidase complex]]
 [[Category: Campbell, M G]]

6bdf

From Proteopedia

Revision as of 10:18, 1 January 2020

2.8 A resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy

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