6q12 - Revision history

OCA at 07:39, 11 October 2023

OCA — Wed, 11 Oct 2023 07:39:22 GMT

←Older revision		Revision as of 07:39, 11 October 2023
Line 3:		Line 3:
	<StructureSection load='6q12' size='340' side='right'caption='[[6q12]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='6q12' size='340' side='right'caption='[[6q12]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6q12]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Staes Staes~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q12 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6Q12 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6q12]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_epidermidis_ATCC_12228 Staphylococcus epidermidis ATCC 12228]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q12 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Q12 FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~>[[6pym\|6pym]]</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]] 2.2Å</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">gseA, esp, SE_1543 ([http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=176280 STAES])</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=6q12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q12 OCA], [https://pdbe.org/6q12 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6q12 RCSB], [https://www.ebi.ac.uk/pdbsum/6q12 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6q12 ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamyl_endopeptidase Glutamyl endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.19 3.4.21.19] </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=6q12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q12 OCA], [~~http~~://pdbe.org/6q12 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6q12 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6q12 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6q12 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/GSEA_STAES GSEA_STAES]] Exhibits a significant hydrolytic activity for the carbonyl side of glutamic acid. Shows activity toward human fibronectin and type 1 collagen (By similarity).	+	[https://www.uniprot.org/uniprot/GSEA_STAES GSEA_STAES] Exhibits a significant hydrolytic activity for the carbonyl side of glutamic acid. Shows activity toward human fibronectin and type 1 collagen (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Glutamyl endopeptidase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Staes~~]]	+	[[Category: Staphylococcus epidermidis ATCC 12228]]
-	[[Category: Manne, K]]	+	[[Category: Manne K]]
-	[[Category: Narayana~~, S V.L]]~~	+	[[Category: Narayana SVL]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Serine protease]]~~	+
-	~~[[Category: Zymogen~~]]	+

OCA at 16:46, 22 January 2020

OCA — Wed, 22 Jan 2020 16:46:51 GMT

←Older revision		Revision as of 16:46, 22 January 2020
Line 11:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/GSEA_STAES GSEA_STAES]] Exhibits a significant hydrolytic activity for the carbonyl side of glutamic acid. Shows activity toward human fibronectin and type 1 collagen (By similarity).		[[http://www.uniprot.org/uniprot/GSEA_STAES GSEA_STAES]] Exhibits a significant hydrolytic activity for the carbonyl side of glutamic acid. Shows activity toward human fibronectin and type 1 collagen (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Extracellular serine protease (Esp) from Staphylococcus epidermidis is a glutamyl endopeptidase that inhibits the growth and formation of S. aureus biofilms. Previously, crystal structures of the matured and active Esp have been determined. Interestingly, many of the staphylococcal glutamyl endopeptidase zymogens, including V8 from Staphylococcus aureus and Esp from S. epidermidis, contain unusually long pro-peptide segments; however, their function is not known. With the aim of elucidating the function of these pro-peptide segments, crystal structures of the Esp zymogen (Pro-Esp) and its variants were determined. It was observed that the N-terminus of the Pro-Esp crystal structure is flexible and is not associated with the main body of the enzyme, unlike in the known active Esp structure. In addition, the loops that border the putative substrate-binding pocket of Pro-Esp are flexible and disordered; the structural components that are responsible for enzyme specificity and efficiency in serine proteases are disordered in Pro-Esp. However, the N-terminal locked Pro-Esp variants exhibit a rigid substrate-binding pocket similar to the active Esp structure and regain activity. These structural studies highlight the role of the N-terminus in stabilizing the structural components responsible for the activity and specificity of staphylococcal glutamyl endopeptidases.
		+
		+	Structural insights into the role of the N-terminus in the activation and function of extracellular serine protease from Staphylococcus epidermidis.,Manne K, Narayana SVL Acta Crystallogr D Struct Biol. 2020 Jan 1;76(Pt 1):28-40. doi:, 10.1107/S2059798319015055. Epub 2020 Jan 1. PMID:31909741<ref>PMID:31909741</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6q12" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 12:36, 18 December 2019

OCA — Wed, 18 Dec 2019 12:36:37 GMT

←Older revision		Revision as of 12:36, 18 December 2019
Line 3:		Line 3:
	<StructureSection load='6q12' size='340' side='right'caption='[[6q12]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='6q12' size='340' side='right'caption='[[6q12]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6q12]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q12 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6q12]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staes Staes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q12 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6pym\|6pym]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6pym\|6pym]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">gseA, esp, SE_1543 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=176280 STAES])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamyl_endopeptidase Glutamyl endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.19 3.4.21.19] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamyl_endopeptidase Glutamyl endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.19 3.4.21.19] </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=6q12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q12 OCA], [http://pdbe.org/6q12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q12 RCSB], [http://www.ebi.ac.uk/pdbsum/6q12 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q12 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=6q12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q12 OCA], [http://pdbe.org/6q12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q12 RCSB], [http://www.ebi.ac.uk/pdbsum/6q12 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q12 ProSAT]</span></td></tr>
Line 14:		Line 15:
	[[Category: Glutamyl endopeptidase]]		[[Category: Glutamyl endopeptidase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
		+	[[Category: Staes]]
	[[Category: Manne, K]]		[[Category: Manne, K]]
	[[Category: Narayana, S V.L]]		[[Category: Narayana, S V.L]]

OCA: Protected "6q12" [edit=sysop:move=sysop]

OCA — Wed, 14 Aug 2019 16:44:15 GMT

Protected "6q12" [edit=sysop:move=sysop]

←Older revision

Revision as of 16:44, 14 August 2019

OCA: New page: ==Structure of pro-Esp mutant- S66V== == Structural highlights == ...

OCA — Wed, 14 Aug 2019 16:44:14 GMT

New page: ==Structure of pro-Esp mutant- S66V== <StructureSection load='6q12' size='340' side='right'caption='6q12, resolution 2.20Å' scene=''> == Structural highlights == ...

New page

==Structure of pro-Esp mutant- S66V==
<StructureSection load='6q12' size='340' side='right'caption='[[6q12]], [[Resolution|resolution]] 2.20Å' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6q12]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q12 OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q12 FirstGlance]. 
</td></tr><tr id='related'><td class="sblockLbl">[[Related_structure|Related:]]</td><td class="sblockDat">[[6pym|6pym]]</td></tr>
<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[http://en.wikipedia.org/wiki/Glutamyl_endopeptidase Glutamyl endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.19 3.4.21.19] </td></tr>
<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6q12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q12 OCA], [http://pdbe.org/6q12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q12 RCSB], [http://www.ebi.ac.uk/pdbsum/6q12 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q12 ProSAT]</td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/GSEA_STAES GSEA_STAES]] Exhibits a significant hydrolytic activity for the carbonyl side of glutamic acid. Shows activity toward human fibronectin and type 1 collagen (By similarity).
__TOC__
</StructureSection>
[[Category: Glutamyl endopeptidase]]
[[Category: Large Structures]]
[[Category: Manne, K]]
[[Category: Narayana, S V.L]]
[[Category: Hydrolase]]
[[Category: Serine protease]]
[[Category: Zymogen]]