We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

3j9i

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:41, 7 February 2024) (edit) (undo)
 
Line 3: Line 3:
<SX load='3j9i' size='340' side='right' viewer='molstar' caption='[[3j9i]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<SX load='3j9i' size='340' side='right' viewer='molstar' caption='[[3j9i]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3j9i]] is a 28 chain structure with sequence from [https://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=3J9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J9I FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3j9i]] is a 28 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J9I FirstGlance]. <br>
-
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pma|1pma]]</div></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">psmA, Ta1288 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970]), psmB, Ta0612 ([https://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'>[https://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3j9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j9i OCA], [https://pdbe.org/3j9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j9i RCSB], [https://www.ebi.ac.uk/pdbsum/3j9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j9i ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3j9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j9i OCA], [https://pdbe.org/3j9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j9i RCSB], [https://www.ebi.ac.uk/pdbsum/3j9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j9i ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/PSA_THEAC 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.<ref>PMID:8999862</ref> [[https://www.uniprot.org/uniprot/PSB_THEAC 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.<ref>PMID:8999862</ref>
+
[https://www.uniprot.org/uniprot/PSA_THEAC 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.<ref>PMID:8999862</ref>
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
In recent work with large high-symmetry viruses, single-particle electron cryomicroscopy (cryo-EM) has achieved the determination of near-atomic-resolution structures by allowing direct fitting of atomic models into experimental density maps. However, achieving this goal with smaller particles of lower symmetry remains challenging. Using a newly developed single electron-counting detector, we confirmed that electron beam-induced motion substantially degrades resolution, and we showed that the combination of rapid readout and nearly noiseless electron counting allow image blurring to be corrected to subpixel accuracy, restoring intrinsic image information to high resolution (Thon rings visible to approximately 3 A). Using this approach, we determined a 3.3-A-resolution structure of an approximately 700-kDa protein with D7 symmetry, the Thermoplasma acidophilum 20S proteasome, showing clear side-chain density. Our method greatly enhances image quality and data acquisition efficiency-key bottlenecks in applying near-atomic-resolution cryo-EM to a broad range of protein samples.
+
-
 
+
-
Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM.,Li X, Mooney P, Zheng S, Booth CR, Braunfeld MB, Gubbens S, Agard DA, Cheng Y Nat Methods. 2013 Jun;10(6):584-90. doi: 10.1038/nmeth.2472. Epub 2013 May 5. PMID:23644547<ref>PMID:23644547</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3j9i" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
Line 28: Line 17:
</SX>
</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Proteasome endopeptidase complex]]
+
[[Category: Thermoplasma acidophilum]]
-
[[Category: Agard, D A]]
+
[[Category: Agard DA]]
-
[[Category: Booth, C]]
+
[[Category: Booth C]]
-
[[Category: Braunfeld, M B]]
+
[[Category: Braunfeld MB]]
-
[[Category: Cheng, Y]]
+
[[Category: Cheng Y]]
-
[[Category: Gubbens, S]]
+
[[Category: Gubbens S]]
-
[[Category: Li, X]]
+
[[Category: Li X]]
-
[[Category: Mooney, P]]
+
[[Category: Mooney P]]
-
[[Category: Zheng, S]]
+
[[Category: Zheng S]]
-
[[Category: Hydrolase]]
+
-
[[Category: Proteasome]]
+

Current revision

Thermoplasma acidophilum 20S proteasome

3j9i, resolution 3.30Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3j9i"
Personal tools