3j9i - Revision history

OCA at 08:41, 7 February 2024

2024-02-07T08:41:19Z

←Older revision		Revision as of 08:41, 7 February 2024
Line 3:		Line 3:
	<SX load='3j9i' size='340' side='right' viewer='molstar' caption='[[3j9i]], [[Resolution\|resolution]] 3.30Å' scene=''>		<SX load='3j9i' size='340' side='right' viewer='molstar' caption='[[3j9i]], [[Resolution\|resolution]] 3.30Å' 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]] 3.3Å</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®/PubMed®, 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~~]]	+

OCA at 13:28, 4 May 2022

2022-05-04T13:28:51Z

←Older revision		Revision as of 13:28, 4 May 2022
Line 3:		Line 3:
	<SX load='3j9i' size='340' side='right' viewer='molstar' caption='[[3j9i]], [[Resolution\|resolution]] 3.30Å' scene=''>		<SX load='3j9i' size='340' side='right' viewer='molstar' caption='[[3j9i]], [[Resolution\|resolution]] 3.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3j9i]] 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=3J9I OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://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_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>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pma\|1pma]]</td></tr>	+	</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>
-	<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='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'>[~~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='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'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=3j9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j9i OCA], [~~http~~://pdbe.org/3j9i PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3j9i RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3j9i PDBsum], [~~http~~://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 ==
-	[[~~http~~://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> [[~~http~~://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> [[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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 18:14, 10 April 2020

2020-04-10T18:14:14Z

←Older revision		Revision as of 18:14, 10 April 2020
Line 3:		Line 3:
	<SX load='3j9i' size='340' side='right' viewer='molstar' caption='[[3j9i]], [[Resolution\|resolution]] 3.30Å' scene=''>		<SX load='3j9i' size='340' side='right' viewer='molstar' caption='[[3j9i]], [[Resolution\|resolution]] 3.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3j9i]] 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=3J9I OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3J9I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3j9i]] 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=3J9I OCA]. For a <b>guided tour on the structure components</b> use [http://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">[[1pma\|1pma]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pma\|1pma]]</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='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='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=3j9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j9i OCA], [http://pdbe.org/3j9i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j9i RCSB], [http://www.ebi.ac.uk/pdbsum/3j9i PDBsum], [http://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'>[http://proteopedia.org/fgij/fg.htm?mol=3j9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j9i OCA], [http://pdbe.org/3j9i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j9i RCSB], [http://www.ebi.ac.uk/pdbsum/3j9i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j9i ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 17:32, 6 March 2020

2020-03-06T17:32:11Z

←Older revision		Revision as of 17:32, 6 March 2020
Line 1:		Line 1:

	==Thermoplasma acidophilum 20S proteasome==		==Thermoplasma acidophilum 20S proteasome==
-	<~~StructureSection~~ load='3j9i' size='340' side='right' caption='[[3j9i]], [[Resolution\|resolution]] 3.30Å' scene=''>	+	<SX load='3j9i' size='340' side='right' viewer='molstar' caption='[[3j9i]], [[Resolution\|resolution]] 3.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3j9i]] 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=3J9I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J9I FirstGlance]. <br>		<table><tr><td colspan='2'>[[3j9i]] 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=3J9I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J9I FirstGlance]. <br>
Line 22:		Line 22:

	==See Also==		==See Also==
-	*[[Proteasome\|Proteasome]]	+	*[[Proteasome 3D structures\|Proteasome 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
		+	[[Category: Large Structures]]
	[[Category: Proteasome endopeptidase complex]]		[[Category: Proteasome endopeptidase complex]]
	[[Category: Agard, D A]]		[[Category: Agard, D A]]

OCA at 08:19, 18 July 2018

2018-07-18T08:19:00Z

←Older revision		Revision as of 08:19, 18 July 2018
Line 3:		Line 3:
	<StructureSection load='3j9i' size='340' side='right' caption='[[3j9i]], [[Resolution\|resolution]] 3.30Å' scene=''>		<StructureSection load='3j9i' size='340' side='right' caption='[[3j9i]], [[Resolution\|resolution]] 3.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3j9i]] is a 28 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J9I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3j9i]] 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=3J9I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J9I FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pma\|1pma]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pma\|1pma]]</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='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=3j9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j9i OCA], [http://pdbe.org/3j9i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j9i RCSB], [http://www.ebi.ac.uk/pdbsum/3j9i PDBsum], [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j9i OCA], [http://pdbe.org/3j9i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j9i RCSB], [http://www.ebi.ac.uk/pdbsum/3j9i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j9i ProSAT]</span></td></tr>

OCA at 20:24, 9 December 2016

2016-12-09T20:24:31Z

←Older revision		Revision as of 20:24, 9 December 2016
Line 1:		Line 1:
		+
	==Thermoplasma acidophilum 20S proteasome==		==Thermoplasma acidophilum 20S proteasome==
	<StructureSection load='3j9i' size='340' side='right' caption='[[3j9i]], [[Resolution\|resolution]] 3.30Å' scene=''>		<StructureSection load='3j9i' size='340' side='right' caption='[[3j9i]], [[Resolution\|resolution]] 3.30Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pma\|1pma]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pma\|1pma]]</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='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=3j9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j9i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j9i RCSB], [http://www.ebi.ac.uk/pdbsum/3j9i PDBsum]</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=3j9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j9i OCA], [http://pdbe.org/3j9i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j9i RCSB], [http://www.ebi.ac.uk/pdbsum/3j9i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j9i ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3j9i" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Proteasome\|Proteasome]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:01, 18 February 2015

2015-02-18T13:01:03Z

←Older revision		Revision as of 13:01, 18 February 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Thermoplasma acidophilum 20S proteasome==
		+	<StructureSection load='3j9i' size='340' side='right' caption='[[3j9i]], [[Resolution\|resolution]] 3.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3j9i]] is a 28 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J9I FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pma\|1pma]]</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=3j9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j9i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j9i RCSB], [http://www.ebi.ac.uk/pdbsum/3j9i PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://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> [[http://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>
		+	<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.

-	~~The entry 3j9i is ON HOLD~~	+	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>

-	~~Authors: Li~~, X.~~, Mooney, P., Zheng,~~ S.~~, Booth, C~~.~~, Braunfeld, M.B., Gubbens, S.,~~ Agard, D.A~~., Cheng, Y.~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Thermoplasma acidophilum 20S proteasome~~	+	== References ==
-	[[Category: ~~Unreleased Structures~~]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Proteasome endopeptidase complex]]
		+	[[Category: Agard, D A]]
		+	[[Category: Booth, C]]
		+	[[Category: Braunfeld, M B]]
	[[Category: Cheng, Y]]		[[Category: Cheng, Y]]
-	[[Category: Booth, C]]
-	[[Category: Zheng, S]]
-	[[Category: Mooney, P]]
	[[Category: Gubbens, S]]		[[Category: Gubbens, S]]
	[[Category: Li, X]]		[[Category: Li, X]]
-	[[Category: ~~Braunfeld~~, ~~M.B~~]]	+	[[Category: Mooney, P]]
-	[[Category: ~~Agard~~, ~~D.A~~]]	+	[[Category: Zheng, S]]
		+	[[Category: Hydrolase]]
		+	[[Category: Proteasome]]

OCA: Protected "3j9i" [edit=sysop:move=sysop]

2015-02-12T06:52:28Z

Protected "3j9i" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:52, 12 February 2015

OCA: New page: '''Unreleased structure''' The entry 3j9i is ON HOLD Authors: Li, X., Mooney, P., Zheng, S., Booth, C., Braunfeld, M.B., Gubbens, S., Agard, D.A., Cheng, Y. Description: Thermoplasma a...

2015-02-12T06:52:27Z

New page: '''Unreleased structure''' The entry 3j9i is ON HOLD Authors: Li, X., Mooney, P., Zheng, S., Booth, C., Braunfeld, M.B., Gubbens, S., Agard, D.A., Cheng, Y. Description: Thermoplasma a...

New page

'''Unreleased structure'''

The entry 3j9i is ON HOLD

Authors: Li, X., Mooney, P., Zheng, S., Booth, C., Braunfeld, M.B., Gubbens, S., Agard, D.A., Cheng, Y.

Description: Thermoplasma acidophilum 20S proteasome
[[Category: Unreleased Structures]]
[[Category: Cheng, Y]]
[[Category: Booth, C]]
[[Category: Zheng, S]]
[[Category: Mooney, P]]
[[Category: Gubbens, S]]
[[Category: Li, X]]
[[Category: Braunfeld, M.B]]
[[Category: Agard, D.A]]