4bug - Revision history

OCA at 11:58, 20 December 2023

2023-12-20T11:58:10Z

← Older revision		Revision as of 11:58, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4bug]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BUG FirstGlance]. <br>		<table><tr><td colspan='2'>[[4bug]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BUG FirstGlance]. <br>
	</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=4bug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bug OCA], [https://pdbe.org/4bug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bug RCSB], [https://www.ebi.ac.uk/pdbsum/4bug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bug ProSAT]</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]] 2.8Å</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=4bug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bug OCA], [https://pdbe.org/4bug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bug RCSB], [https://www.ebi.ac.uk/pdbsum/4bug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bug ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/Q8GRA2_STRPY Q8GRA2_STRPY]]		[https://www.uniprot.org/uniprot/Q8GRA2_STRPY Q8GRA2_STRPY]
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Streptococcus pyogenes and other Gram-positive bacterial pathogens present long macromolecular filaments known as pili on their surface that mediate adhesion and colonization. These pili are covalent polymers, assembled by sortases. Typically, they comprise a putative adhesin at their tip, a backbone subunit present in multiple copies and a basal subunit that is covalently anchored to the peptidoglycan layer of the cell surface. The crystal structures of pilin subunits revealed the presence of unusual covalent linkages in these proteins, including intramolecular isopeptide and internal thioester bonds. The intramolecular isopeptide bonds in backbone pilins are important for protein stability. Here, using both the wild-type protein and a set of mutants, we assessed the proteolytic and thermal stability of the S. pyogenes pilus tip adhesin Spy0125, in the presence and absence of its intramolecular isopeptide and internal thioester bonds. We also determined a crystal structure of the internal thioester bond variant Spy0125Cys426Ala . We find that mutations in the intramolecular isopeptide bonds compromise the stability of Spy0125. Using limited proteolysis and thermal denaturation assays, we could separate the contribution of each intramolecular isopeptide bond to Spy0125 stability. In contrast, mutation in the internal thioester bond had a lesser effect on protein stability and the crystal structure is essentially identical to wild type. This work suggests that the internal thioester in Spy0125, although having a minor contributory role, is not required for protein stability and must have a different primary function, most likely mediating a covalent interaction with host cell ligands. Proteins 2013; (c) 2013 Wiley Periodicals, Inc.

			Intramolecular isopeptide but not internal thioester bonds confer proteolytic and significant thermal stability to the S. pyogenes pilus adhesin Spy0125.,Walden M, Crow A, Nelson MD, Banfield MJ Proteins. 2013 Sep 30. doi: 10.1002/prot.24420. PMID:24123467<ref>PMID:24123467</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 4bug" style="background-color:#fffaf0;"></div>
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:08, 7 September 2022

2022-09-07T17:08:45Z

← Older revision		Revision as of 17:08, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4bug' size='340' side='right'caption='[[4bug]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='4bug' size='340' side='right'caption='[[4bug]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4bug]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"micrococcus_scarlatinae"_klein_1884 "micrococcus scarlatinae" klein 1884~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4BUG FirstGlance]. <br>		<table><tr><td colspan='2'>[[4bug]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BUG FirstGlance]. <br>
	</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=4bug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bug OCA], [~~http~~://pdbe.org/4bug PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4bug RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4bug PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4bug ProSAT]</span></td></tr>		</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=4bug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bug OCA], [https://pdbe.org/4bug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bug RCSB], [https://www.ebi.ac.uk/pdbsum/4bug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bug ProSAT]</span></td></tr>
	</table>		</table>
	~~<div style="background-color:#fffaf0;">~~		== Function ==
	== ~~Publication Abstract from PubMed~~ ==		[[https://www.uniprot.org/uniprot/Q8GRA2_STRPY Q8GRA2_STRPY]]
	Streptococcus pyogenes and other Gram-positive bacterial pathogens present long macromolecular filaments known as pili on their surface that mediate adhesion and colonization. These pili are covalent polymers, assembled by sortases. Typically, they comprise a putative adhesin at their tip, a backbone subunit present in multiple copies and a basal subunit that is covalently anchored to the peptidoglycan layer of the cell surface. The crystal structures of pilin subunits revealed the presence of unusual covalent linkages in these proteins, including intramolecular isopeptide and internal thioester bonds. The intramolecular isopeptide bonds in backbone pilins are important for protein stability. Here, using both the wild-type protein and a set of mutants, we assessed the proteolytic and thermal stability of the S. pyogenes pilus tip adhesin Spy0125, in the presence and absence of its intramolecular isopeptide and internal thioester bonds. We also determined a crystal structure of the internal thioester bond variant Spy0125Cys426Ala . We find that mutations in the intramolecular isopeptide bonds compromise the stability of Spy0125. Using limited proteolysis and thermal denaturation assays, we could separate the contribution of each intramolecular isopeptide bond to Spy0125 stability. In contrast, mutation in the internal thioester bond had a lesser effect on protein stability and the crystal structure is essentially identical to wild type. This work suggests that the internal thioester in Spy0125, although having a minor contributory role, is not required for protein stability and must have a different primary function, most likely mediating a covalent interaction with host cell ligands. Proteins 2013; (c) 2013 Wiley Periodicals, Inc.

	Intramolecular isopeptide but not internal thioester bonds confer proteolytic and significant thermal stability to the S. pyogenes pilus adhesin Spy0125.,Walden M, Crow A, Nelson MD, Banfield MJ Proteins. 2013 Sep 30. doi: ~~10.1002~~/~~prot.24420. PMID:24123467<ref>PMID:24123467<~~/~~ref>~~

	~~From MEDLINE®/PubMed®, a database of the U~~.S. ~~National Library of Medicine.<br>~~
	</~~div>~~
	~~<div class="pdbe-citations 4bug" style="background-color:#fffaf0;"></div>~~
	~~== References ==~~
	~~<references~~/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Micrococcus scarlatinae klein 1884]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Banfield, M J~~]]		[[Category: Streptococcus pyogenes]]
	[[Category: ~~Crow, A~~]]		[[Category: Banfield MJ]]
	[[Category: ~~Nelson, M~~]]		[[Category: Crow A]]
	[[Category: ~~Walden,~~ M]]		[[Category: Nelson M]]
	[[Category: ~~Cell adhesion~~]]		[[Category: Walden M]]

OCA at 13:54, 13 March 2019

2019-03-13T13:54:23Z

← Older revision		Revision as of 13:54, 13 March 2019
Line 1:		Line 1:

	==Pilus-presented adhesin, Spy0125 (Cpa), Cys426Ala mutant==		==Pilus-presented adhesin, Spy0125 (Cpa), Cys426Ala mutant==
	<StructureSection load='4bug' size='340' side='right' caption='[[4bug]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='4bug' size='340' side='right'caption='[[4bug]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4bug]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_scarlatinae"_klein_1884 "micrococcus scarlatinae" klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BUG FirstGlance]. <br>		<table><tr><td colspan='2'>[[4bug]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_scarlatinae"_klein_1884 "micrococcus scarlatinae" klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BUG FirstGlance]. <br>
Line 20:		Line 20:
	</StructureSection>		</StructureSection>
	[[Category: Micrococcus scarlatinae klein 1884]]		[[Category: Micrococcus scarlatinae klein 1884]]
			[[Category: Large Structures]]
	[[Category: Banfield, M J]]		[[Category: Banfield, M J]]
	[[Category: Crow, A]]		[[Category: Crow, A]]

OCA at 19:54, 4 August 2016

2016-08-04T19:54:46Z

← Older revision		Revision as of 19:54, 4 August 2016
Line 1:		Line 1:

	==Pilus-presented adhesin, Spy0125 (Cpa), Cys426Ala mutant==		==Pilus-presented adhesin, Spy0125 (Cpa), Cys426Ala mutant==
	<StructureSection load='4bug' size='340' side='right' caption='[[4bug]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='4bug' size='340' side='right' caption='[[4bug]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4bug]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_scarlatinae"_klein_1884 "micrococcus scarlatinae" klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BUG FirstGlance]. <br>		<table><tr><td colspan='2'>[[4bug]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_scarlatinae"_klein_1884 "micrococcus scarlatinae" klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BUG FirstGlance]. <br>
	</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=4bug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bug OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bug RCSB], [http://www.ebi.ac.uk/pdbsum/4bug PDBsum]</span></td></tr>		</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=4bug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bug OCA], [http://pdbe.org/4bug PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bug RCSB], [http://www.ebi.ac.uk/pdbsum/4bug PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bug ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 13:		Line 14:
	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 4bug" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:30, 21 December 2014

2014-12-21T17:30:39Z

← Older revision		Revision as of 17:30, 21 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_4bug\| PDB=4bug \| SCENE= }}~~		==Pilus-presented adhesin, Spy0125 (Cpa), Cys426Ala mutant==
	===Pilus-presented adhesin, Spy0125 (Cpa), Cys426Ala mutant===		<StructureSection load='4bug' size='340' side='right' caption='[[4bug]], [[Resolution\|resolution]] 2.80Å' scene=''>
	~~{{ABSTRACT_PUBMED_24123467}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4bug]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_scarlatinae"_klein_1884 "micrococcus scarlatinae" klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BUG FirstGlance]. <br>
			</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=4bug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bug OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bug RCSB], [http://www.ebi.ac.uk/pdbsum/4bug PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Streptococcus pyogenes and other Gram-positive bacterial pathogens present long macromolecular filaments known as pili on their surface that mediate adhesion and colonization. These pili are covalent polymers, assembled by sortases. Typically, they comprise a putative adhesin at their tip, a backbone subunit present in multiple copies and a basal subunit that is covalently anchored to the peptidoglycan layer of the cell surface. The crystal structures of pilin subunits revealed the presence of unusual covalent linkages in these proteins, including intramolecular isopeptide and internal thioester bonds. The intramolecular isopeptide bonds in backbone pilins are important for protein stability. Here, using both the wild-type protein and a set of mutants, we assessed the proteolytic and thermal stability of the S. pyogenes pilus tip adhesin Spy0125, in the presence and absence of its intramolecular isopeptide and internal thioester bonds. We also determined a crystal structure of the internal thioester bond variant Spy0125Cys426Ala . We find that mutations in the intramolecular isopeptide bonds compromise the stability of Spy0125. Using limited proteolysis and thermal denaturation assays, we could separate the contribution of each intramolecular isopeptide bond to Spy0125 stability. In contrast, mutation in the internal thioester bond had a lesser effect on protein stability and the crystal structure is essentially identical to wild type. This work suggests that the internal thioester in Spy0125, although having a minor contributory role, is not required for protein stability and must have a different primary function, most likely mediating a covalent interaction with host cell ligands. Proteins 2013; (c) 2013 Wiley Periodicals, Inc.

	~~==About this Structure==~~		Intramolecular isopeptide but not internal thioester bonds confer proteolytic and significant thermal stability to the S. pyogenes pilus adhesin Spy0125.,Walden M, Crow A, Nelson MD, Banfield MJ Proteins. 2013 Sep 30. doi: 10.1002/prot.24420. PMID:24123467<ref>PMID:24123467</ref>
	~~[[4bug]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/"micrococcus_scarlatinae"_klein_1884 "micrococcus scarlatinae" klein 1884]~~. ~~Full crystallographic information is available from [http~~:/~~/oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4BUG OCA].~~

	==~~Reference~~==		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~<ref group="xtra">PMID:024123467</ref>~~<references ~~group="xtra"~~/><~~references~~/>		</div>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
	[[Category: Micrococcus scarlatinae klein 1884]]		[[Category: Micrococcus scarlatinae klein 1884]]
	[[Category: Banfield, M J.]]		[[Category: Banfield, M J]]
	[[Category: Crow, A.]]		[[Category: Crow, A]]
	[[Category: Nelson, M.]]		[[Category: Nelson, M]]
	[[Category: Walden, M.]]		[[Category: Walden, M]]
	[[Category: Cell adhesion]]		[[Category: Cell adhesion]]

OCA at 15:01, 19 February 2014

2014-02-19T15:01:38Z

← Older revision		Revision as of 15:01, 19 February 2014
Line 4:		Line 4:

	==About this Structure==		==About this Structure==
	[[4bug]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Streptococcus_pyogenes Streptococcus pyogenes~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUG OCA].		[[4bug]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_scarlatinae"_klein_1884 "micrococcus scarlatinae" klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUG OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:024123467</ref><references group="xtra"/><references/>		<ref group="xtra">PMID:024123467</ref><references group="xtra"/><references/>
	[[Category: ~~Streptococcus pyogenes~~]]		[[Category: Micrococcus scarlatinae klein 1884]]
	[[Category: Banfield, M J.]]		[[Category: Banfield, M J.]]
	[[Category: Crow, A.]]		[[Category: Crow, A.]]

OCA at 05:13, 23 October 2013

2013-10-23T05:13:44Z

← Older revision		Revision as of 05:13, 23 October 2013
Line 1:		Line 1:
	{{STRUCTURE_4bug\| PDB=4bug \| SCENE= }}		{{STRUCTURE_4bug\| PDB=4bug \| SCENE= }}
	===Pilus-presented adhesin, Spy0125 (Cpa), Cys426Ala mutant===		===Pilus-presented adhesin, Spy0125 (Cpa), Cys426Ala mutant===
			{{ABSTRACT_PUBMED_24123467}}

	==About this Structure==		==About this Structure==
	[[4bug]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUG OCA].		[[4bug]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUG OCA].

			==Reference==
			<ref group="xtra">PMID:024123467</ref><references group="xtra"/><references/>
	[[Category: Streptococcus pyogenes]]		[[Category: Streptococcus pyogenes]]
	[[Category: Banfield, M J.]]		[[Category: Banfield, M J.]]

OCA at 06:34, 10 October 2013

2013-10-10T06:34:31Z

← Older revision		Revision as of 06:34, 10 October 2013
Line 1:		Line 1:
	~~'''Unreleased structure'''~~		{{STRUCTURE_4bug\| PDB=4bug \| SCENE= }}
			===Pilus-presented adhesin, Spy0125 (Cpa), Cys426Ala mutant===

	~~The entry~~ 4bug is ~~ON HOLD until Paper Publication~~		==About this Structure==
			[[4bug]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUG OCA].
	~~Authors~~: ~~Walden~~, M., Crow, A., Nelson, M.~~, Banfield~~, M.J.		[[Category: Streptococcus pyogenes]]
			[[Category: Banfield, M J.]]
	~~Description~~: ~~Pilus-presented adhesin, Spy0125 (Cpa), Cys426Ala mutant~~		[[Category: Crow, A.]]
			[[Category: Nelson, M.]]
			[[Category: Walden, M.]]
			[[Category: Cell adhesion]]

OCA at 03:16, 20 September 2013

2013-09-20T03:16:24Z

← Older revision		Revision as of 03:16, 20 September 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4bug is ON HOLD		The entry 4bug is ON HOLD until Paper Publication

	Authors: Walden, M., Crow, A., Nelson, M., Banfield, M.J.		Authors: Walden, M., Crow, A., Nelson, M., Banfield, M.J.

	Description: Pilus-presented adhesin, Spy0125 (Cpa), Cys426Ala mutant		Description: Pilus-presented adhesin, Spy0125 (Cpa), Cys426Ala mutant

OCA: Protected "4bug" [edit=sysop:move=sysop]

2013-06-30T08:31:01Z

Protected "4bug" [edit=sysop:move=sysop]

← Older revision	Revision as of 08:31, 30 June 2013
(No difference)