6iqs - Revision history

OCA at 09:51, 22 November 2023

OCA — Wed, 22 Nov 2023 09:51:10 GMT

←Older revision		Revision as of 09:51, 22 November 2023
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	<StructureSection load='6iqs' size='340' side='right'caption='[[6iqs]], [[Resolution\|resolution]] 2.69Å' scene=''>		<StructureSection load='6iqs' size='340' side='right'caption='[[6iqs]], [[Resolution\|resolution]] 2.69Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6iqs]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IQS OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6IQS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6iqs]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IQS FirstGlance]. <br>
-	</td></tr><tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"~~><span class~~=~~'plainlinks'~~>~~[http://en.wikipedia.org/wiki/C~~-~~terminal_processing_peptidase C-terminal processing peptidase]~~, ~~with EC number~~ [~~http://www~~.~~brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.102 3.4.21.102] </span>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.69Å</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=6iqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iqs OCA], [~~http~~://pdbe.org/6iqs PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6iqs RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6iqs PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6iqs 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=6iqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iqs OCA], [https://pdbe.org/6iqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iqs RCSB], [https://www.ebi.ac.uk/pdbsum/6iqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iqs ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/NLPI_ECOLI NLPI_ECOLI]] May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division. Negatively controls the production of extracellular DNA (eDNA).<ref>PMID:10400590</ref> <ref>PMID:20833130</ref> ~~[[http~~:~~//www~~.~~uniprot~~.~~org/uniprot/PRC_ECOLI PRC_ECOLI]] Involved in~~ the ~~cleavage~~ of a C-~~terminal peptide~~ of ~~11 residues~~ from the ~~precursor form~~ of ~~penicillin~~-~~binding protein 3~~ (~~PBP3~~). ~~May be involved~~ in ~~protection~~ of the ~~bacterium from thermal and osmotic stresses~~.	+	[https://www.uniprot.org/uniprot/NLPI_ECOLI NLPI_ECOLI] May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division. Negatively controls the production of extracellular DNA (eDNA).<ref>PMID:10400590</ref> <ref>PMID:20833130</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Carboxyl (C)-terminal processing proteases (CTPs) participate in protective and regulatory proteolysis in bacteria. The PDZ domain is central to the activity of CTPs but plays inherently different regulatory roles. For example, the PDZ domain inhibits the activity of the signaling protease CtpB by blocking the active site but is required for the activation of Prc (or Tsp), a tail-specific protease that degrades SsrA-tagged proteins. Here, by structural and functional analyses, we show that in the unliganded resting state of Prc, the PDZ domain is docked inside the bowl-shaped scaffold without contacting the active site, which is kept in a default misaligned conformation. In Prc, a hydrophobic substrate sensor distinct from CtpB engages substrate binding to the PDZ domain and triggers a structural remodeling to align the active-site residues. Therefore, this work reveals the structural basis for understanding the contrasting roles of the PDZ domain in the regulation of CTPs.IMPORTANCE Prc, also known previously as Tsp, is the founding member of the carboxyl-terminal processing protease (CTP) family of PDZ domain-containing proteases that include CtpA and CtpB. The substrate-binding PDZ domain is responsible for regulating the protease activity of CTP proteases; however, the regulatory role of PDZ domain is stimulatory in Prc but inhibitory in CtpA/B. By determining a series of crystal structures of Prc in the unliganded resting state, this study presents the structural basis for PDZ-dependent activation of Prc, the results of which explain the contrasting roles of the PDZ domain in the regulation of the protease activity of CTPs.
		+
		+	Structural Basis for the Differential Regulatory Roles of the PDZ Domain in C-Terminal Processing Proteases.,Chueh CK, Som N, Ke LC, Ho MR, Reddy M, Chang CI mBio. 2019 Aug 6;10(4):e01129-19. doi: 10.1128/mBio.01129-19. PMID:31387902<ref>PMID:31387902</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6iqs" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: C-~~terminal processing peptidase~~]]	+	[[Category: Escherichia coli K-12]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Chang~~, C I~~]]	+	[[Category: Chang CI]]
-	[[Category: Chuech~~, C K]]~~	+	[[Category: Chuech CK]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Peptidoglycan remodeling]]~~	+
-	~~[[Category: Protein quality control~~]]	+

OCA at 06:11, 24 July 2019

OCA — Wed, 24 Jul 2019 06:11:43 GMT

←Older revision		Revision as of 06:11, 24 July 2019
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-	'''Unreleased structure'''

-	~~The entry~~ 6iqs is ~~ON HOLD until Paper Publication~~	+	==Crystal structure of Prc with L245A and L340G mutations in complex with NlpI==
-		+	<StructureSection load='6iqs' size='340' side='right'caption='[[6iqs]], [[Resolution\|resolution]] 2.69Å' scene=''>
-	~~Authors~~: ~~Chuech~~, C.K., ~~Chang~~, C.I.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6iqs]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IQS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IQS FirstGlance]. <br>
-	~~Description~~: ~~Crystal structure~~ of ~~Prc with L245A and L340G mutations~~ in ~~complex with NlpI~~	+	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/C-terminal_processing_peptidase C-terminal processing peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.102 3.4.21.102] </span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	<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=6iqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iqs OCA], [http://pdbe.org/6iqs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6iqs RCSB], [http://www.ebi.ac.uk/pdbsum/6iqs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6iqs ProSAT]</span></td></tr>
-	[[Category: ~~Chuech~~, C.K]]	+	</table>
-	[[Category: ~~Chang~~, C.I]]	+	== Function ==
		+	[[http://www.uniprot.org/uniprot/NLPI_ECOLI NLPI_ECOLI]] May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division. Negatively controls the production of extracellular DNA (eDNA).<ref>PMID:10400590</ref> <ref>PMID:20833130</ref> [[http://www.uniprot.org/uniprot/PRC_ECOLI PRC_ECOLI]] Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses.
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: C-terminal processing peptidase]]
		+	[[Category: Large Structures]]
		+	[[Category: Chang, C I]]
		+	[[Category: Chuech, C K]]
		+	[[Category: Hydrolase]]
		+	[[Category: Peptidoglycan remodeling]]
		+	[[Category: Protein quality control]]

OCA at 05:08, 5 December 2018

OCA — Wed, 05 Dec 2018 05:08:53 GMT

←Older revision		Revision as of 05:08, 5 December 2018
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6iqs is ON HOLD	+	The entry 6iqs is ON HOLD until Paper Publication

	Authors: Chuech, C.K., Chang, C.I.		Authors: Chuech, C.K., Chang, C.I.
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	Description: Crystal structure of Prc with L245A and L340G mutations in complex with NlpI		Description: Crystal structure of Prc with L245A and L340G mutations in complex with NlpI
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Chang, C.I]]
	[[Category: Chuech, C.K]]		[[Category: Chuech, C.K]]
		+	[[Category: Chang, C.I]]

OCA: Protected "6iqs" [edit=sysop:move=sysop]

OCA — Wed, 14 Nov 2018 06:34:40 GMT

Protected "6iqs" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:34, 14 November 2018

OCA: New page: '''Unreleased structure''' The entry 6iqs is ON HOLD Authors: Chuech, C.K., Chang, C.I. Description: Crystal structure of Prc with L245A and L340G mutations in complex with NlpI [[Cate...

OCA — Wed, 14 Nov 2018 06:34:38 GMT

New page: '''Unreleased structure''' The entry 6iqs is ON HOLD Authors: Chuech, C.K., Chang, C.I. Description: Crystal structure of Prc with L245A and L340G mutations in complex with NlpI [[Cate...

New page

'''Unreleased structure'''

The entry 6iqs is ON HOLD

Authors: Chuech, C.K., Chang, C.I.

Description: Crystal structure of Prc with L245A and L340G mutations in complex with NlpI
[[Category: Unreleased Structures]]
[[Category: Chang, C.I]]
[[Category: Chuech, C.K]]