5vy4

From Proteopedia

(Difference between revisions)

Revision as of 22:14, 10 April 2020

Thermoplasma acidophilum 20S Proteasome using 200keV with image shift

5vy4, resolution 3.30Å

Structural highlights

5vy4 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
Experimental data:	Check to display Experimental Data
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

Nearly all single-particle cryo-EM structures resolved to better than 4-A resolution have been determined using 300-keV transmission electron microscopes (TEMs). We demonstrate that it is possible to obtain reconstructions of macromolecular complexes of different sizes to better than 3-A resolution using a 200-keV TEM. These structures are of sufficient quality to unambiguously assign amino acid rotameric conformations and identify ordered water molecules.

Achieving better-than-3-A resolution by single-particle cryo-EM at 200 keV.,Herzik MA Jr, Wu M, Lander GC Nat Methods. 2017 Oct 9. doi: 10.1038/nmeth.4461. PMID:28991891^[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
↑ Herzik MA Jr, Wu M, Lander GC. Achieving better-than-3-A resolution by single-particle cryo-EM at 200 keV. Nat Methods. 2017 Oct 9. doi: 10.1038/nmeth.4461. PMID:28991891 doi:http://dx.doi.org/10.1038/nmeth.4461

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/5vy4"

@@ Line 3: / Line 3: @@
 <SX load='5vy4' size='340' side='right' viewer='molstar' caption='[[5vy4]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5vy4]] 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=5VY4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VY4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5vy4]] 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=5VY4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5VY4 FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">psmA, Ta1288 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970]), psmB, Ta0612 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</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=5vy4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vy4 OCA], [http://pdbe.org/5vy4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vy4 RCSB], [http://www.ebi.ac.uk/pdbsum/5vy4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vy4 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=5vy4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vy4 OCA], [http://pdbe.org/5vy4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vy4 RCSB], [http://www.ebi.ac.uk/pdbsum/5vy4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vy4 ProSAT]</span></td></tr>
 </table>
 == Function ==

5vy4

From Proteopedia

Revision as of 22:14, 10 April 2020

Thermoplasma acidophilum 20S Proteasome using 200keV with image shift

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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