5h3w - Revision history

OCA at 09:14, 20 March 2024

OCA — Wed, 20 Mar 2024 09:14:55 GMT

←Older revision		Revision as of 09:14, 20 March 2024
Line 9:		Line 9:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/RQCH_STRSY RQCH_STRSY] Part of the ribosome quality control system (RQC). Recruits Ala-charged tRNA and directs the elongation of stalled nascent chains on 50S ribosomal subunits, leading to non-templated C-terminal Ala extensions (Ala tail). The Ala tail promotes nascent chain degradation. May add between 1 and at least 8 Ala residues. Binds to stalled 50S ribosomal subunits.[HAMAP-Rule:MF_00844]		[https://www.uniprot.org/uniprot/RQCH_STRSY RQCH_STRSY] Part of the ribosome quality control system (RQC). Recruits Ala-charged tRNA and directs the elongation of stalled nascent chains on 50S ribosomal subunits, leading to non-templated C-terminal Ala extensions (Ala tail). The Ala tail promotes nascent chain degradation. May add between 1 and at least 8 Ala residues. Binds to stalled 50S ribosomal subunits.[HAMAP-Rule:MF_00844]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The anchorless fibronectin-binding proteins (FnBPs) are a group of important virulence factors for which the structures are not available and the functions are not well defined. In this study we performed comprehensive studies on a prototypic member of this group: the fibronectin-/fibrinogen-binding protein from Streptococcus suis (FBPS). The structures of the N- and C-terminal halves (FBPS-N and FBPS-C), which together cover the full-length protein in sequence, were solved at a resolution of 2.1 and 2.6 A, respectively, and each was found to be composed of two domains with unique folds. Furthermore, we have elucidated the organization of these domains by small-angle X-ray scattering. We further showed that the fibronectin-binding site is located in FBPS-C and that FBPS promotes the adherence of S suis to host cells by attaching the bacteria via FBPS-N. Finally, we demonstrated that FBPS functions both as an adhesin, promoting S suis attachment to host cells, and as a bacterial factor, activating signaling pathways via beta1 integrin receptors to induce chemokine production.
-
-	Structural and functional analysis of an anchorless fibronectin-binding protein FBPS from Gram-positive bacterium Streptococcus suis.,Musyoki AM, Shi Z, Xuan C, Lu G, Qi J, Gao F, Zheng B, Zhang Q, Li Y, Haywood J, Liu C, Yan J, Shi Y, Gao GF Proc Natl Acad Sci U S A. 2016 Nov 29;113(48):13869-13874. Epub 2016 Nov 10. PMID:27834729<ref>PMID:27834729</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5h3w" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 07:22, 9 August 2023

OCA — Wed, 09 Aug 2023 07:22:57 GMT

←Older revision		Revision as of 07:22, 9 August 2023
Line 3:		Line 3:
	<StructureSection load='5h3w' size='340' side='right'caption='[[5h3w]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='5h3w' size='340' side='right'caption='[[5h3w]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5h3w]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Atcc_43765 Atcc 43765~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H3W OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5H3W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5h3w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_suis Streptococcus suis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H3W FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~>[[5h3x\|5h3x]]</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]] 2.6Å</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">fbps ([http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=1307 ATCC 43765])~~</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=5h3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h3w OCA], [https://pdbe.org/5h3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h3w RCSB], [https://www.ebi.ac.uk/pdbsum/5h3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h3w 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=5h3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h3w OCA], [~~http~~://pdbe.org/5h3w PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5h3w RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5h3w PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5h3w ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/RQCH_STRSY RQCH_STRSY] Part of the ribosome quality control system (RQC). Recruits Ala-charged tRNA and directs the elongation of stalled nascent chains on 50S ribosomal subunits, leading to non-templated C-terminal Ala extensions (Ala tail). The Ala tail promotes nascent chain degradation. May add between 1 and at least 8 Ala residues. Binds to stalled 50S ribosomal subunits.[HAMAP-Rule:MF_00844]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 43765]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Gao, G F~~]]	+	[[Category: Streptococcus suis]]
-	[[Category: ~~Musyoki, A M~~]]	+	[[Category: Gao GF]]
-	[[Category: ~~Qi, J~~]]	+	[[Category: Musyoki AM]]
-	[[Category: ~~Cell adhesion]]~~	+	[[Category: Qi J]]
-	~~[[Category: Fibronectin-binding property]]~~	+
-	~~[[Category: Novel fold~~]]	+

OCA at 06:52, 20 May 2020

OCA — Wed, 20 May 2020 06:52:00 GMT

←Older revision		Revision as of 06:52, 20 May 2020
Line 1:		Line 1:

	==The structure of the C-terminal of the fibronectin/fibrinogen-binding protein from Streptococcus suis (FBPS)==		==The structure of the C-terminal of the fibronectin/fibrinogen-binding protein from Streptococcus suis (FBPS)==
-	<StructureSection load='5h3w' size='340' side='right' caption='[[5h3w]], [[Resolution\|resolution]] 2.60Å' scene=''>	+	<StructureSection load='5h3w' size='340' side='right'caption='[[5h3w]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5h3w]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H3W OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5H3W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5h3w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43765 Atcc 43765]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H3W OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5H3W FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5h3x\|5h3x]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5h3x\|5h3x]]</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=5h3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h3w OCA], [http://pdbe.org/5h3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h3w RCSB], [http://www.ebi.ac.uk/pdbsum/5h3w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h3w ProSAT]</span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fbps ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1307 ATCC 43765])</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=5h3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h3w OCA], [http://pdbe.org/5h3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h3w RCSB], [http://www.ebi.ac.uk/pdbsum/5h3w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h3w ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 20:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Atcc 43765]]
		+	[[Category: Large Structures]]
	[[Category: Gao, G F]]		[[Category: Gao, G F]]
	[[Category: Musyoki, A M]]		[[Category: Musyoki, A M]]

OCA at 11:19, 15 December 2016

OCA — Thu, 15 Dec 2016 11:19:10 GMT

←Older revision		Revision as of 11:19, 15 December 2016
Line 7:		Line 7:
	<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=5h3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h3w OCA], [http://pdbe.org/5h3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h3w RCSB], [http://www.ebi.ac.uk/pdbsum/5h3w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h3w 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=5h3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h3w OCA], [http://pdbe.org/5h3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h3w RCSB], [http://www.ebi.ac.uk/pdbsum/5h3w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h3w ProSAT]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The anchorless fibronectin-binding proteins (FnBPs) are a group of important virulence factors for which the structures are not available and the functions are not well defined. In this study we performed comprehensive studies on a prototypic member of this group: the fibronectin-/fibrinogen-binding protein from Streptococcus suis (FBPS). The structures of the N- and C-terminal halves (FBPS-N and FBPS-C), which together cover the full-length protein in sequence, were solved at a resolution of 2.1 and 2.6 A, respectively, and each was found to be composed of two domains with unique folds. Furthermore, we have elucidated the organization of these domains by small-angle X-ray scattering. We further showed that the fibronectin-binding site is located in FBPS-C and that FBPS promotes the adherence of S suis to host cells by attaching the bacteria via FBPS-N. Finally, we demonstrated that FBPS functions both as an adhesin, promoting S suis attachment to host cells, and as a bacterial factor, activating signaling pathways via beta1 integrin receptors to induce chemokine production.
		+
		+	Structural and functional analysis of an anchorless fibronectin-binding protein FBPS from Gram-positive bacterium Streptococcus suis.,Musyoki AM, Shi Z, Xuan C, Lu G, Qi J, Gao F, Zheng B, Zhang Q, Li Y, Haywood J, Liu C, Yan J, Shi Y, Gao GF Proc Natl Acad Sci U S A. 2016 Nov 29;113(48):13869-13874. Epub 2016 Nov 10. PMID:27834729<ref>PMID:27834729</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5h3w" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 03:25, 10 December 2016

OCA — Sat, 10 Dec 2016 03:25:23 GMT

←Older revision		Revision as of 03:25, 10 December 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry 5h3w is ON HOLD~~	+	==The structure of the C-terminal of the fibronectin/fibrinogen-binding protein from Streptococcus suis (FBPS)==
-		+	<StructureSection load='5h3w' size='340' side='right' caption='[[5h3w]], [[Resolution\|resolution]] 2.60Å' scene=''>
-	~~Authors: Musyoki, A.M., Qi, J., Gao, G.F.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5h3w]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H3W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H3W FirstGlance]. <br>
-	~~Description:~~ The structure of the C-terminal of the fibronectin/fibrinogen-binding protein from Streptococcus suis (FBPS)	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5h3x\|5h3x]]</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=5h3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h3w OCA], [http://pdbe.org/5h3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h3w RCSB], [http://www.ebi.ac.uk/pdbsum/5h3w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h3w ProSAT]</span></td></tr>
-	[[Category: Gao, G.F]]	+	</table>
-	[[Category: Musyoki, A.M]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Gao, G F]]
		+	[[Category: Musyoki, A M]]
	[[Category: Qi, J]]		[[Category: Qi, J]]
		+	[[Category: Cell adhesion]]
		+	[[Category: Fibronectin-binding property]]
		+	[[Category: Novel fold]]

OCA: Protected "5h3w" [edit=sysop:move=sysop]

OCA — Wed, 02 Nov 2016 12:57:53 GMT

Protected "5h3w" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:57, 2 November 2016

OCA: New page: '''Unreleased structure''' The entry 5h3w is ON HOLD Authors: Musyoki, A.M., Qi, J., Gao, G.F. Description: The structure of the C-terminal of the fibronectin/fibrinogen-binding protei...

OCA — Wed, 02 Nov 2016 12:57:51 GMT

New page: '''Unreleased structure''' The entry 5h3w is ON HOLD Authors: Musyoki, A.M., Qi, J., Gao, G.F. Description: The structure of the C-terminal of the fibronectin/fibrinogen-binding protei...

New page

'''Unreleased structure'''

The entry 5h3w is ON HOLD

Authors: Musyoki, A.M., Qi, J., Gao, G.F.

Description: The structure of the C-terminal of the fibronectin/fibrinogen-binding protein from Streptococcus suis (FBPS)
[[Category: Unreleased Structures]]
[[Category: Gao, G.F]]
[[Category: Musyoki, A.M]]
[[Category: Qi, J]]