8ec3 - Revision history

OCA at 07:26, 3 April 2024

2024-04-03T07:26:24Z

←Older revision		Revision as of 07:26, 3 April 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[8ec3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Borrelia_hermsii_HS1 Borrelia hermsii HS1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EC3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[8ec3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Borrelia_hermsii_HS1 Borrelia hermsii HS1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EC3 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 1.5Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=8ec3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ec3 OCA], [https://pdbe.org/8ec3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ec3 RCSB], [https://www.ebi.ac.uk/pdbsum/8ec3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ec3 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=8ec3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ec3 OCA], [https://pdbe.org/8ec3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ec3 RCSB], [https://www.ebi.ac.uk/pdbsum/8ec3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ec3 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/G9BXS5_BORHE G9BXS5_BORHE]		[https://www.uniprot.org/uniprot/G9BXS5_BORHE G9BXS5_BORHE]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Borrelial pathogens are vector-borne etiological agents of Lyme disease, relapsing fever, and Borrelia miyamotoi disease. These spirochetes each encode several surface-localized lipoproteins that bind to components of the human complement system. BBK32 is an example of a borrelial lipoprotein that protects the Lyme disease spirochete from complement-mediated attack. The complement inhibitory activity of BBK32 arises from an alpha helical C-terminal domain that interacts directly with the initiating protease of the classical pathway, C1r. Borrelia miyamotoi spirochetes encode BBK32 orthologs termed FbpA and FbpB, and these proteins also inhibit C1r, albeit via distinct recognition mechanisms. The C1r-inhibitory activities of a third ortholog termed FbpC, which is found exclusively in relapsing fever spirochetes, remains unknown. Here we report the crystal structure of the C-terminal domain of B. hermsii FbpC to a limiting resolution of 1.5 A. Surface plasmon resonance studies and assays of complement function demonstrate that FbpC retains potent BBK32-like anti-complement activities. Based on the structure of FbpC, we hypothesized that conformational dynamics of the complement inhibitory domains of borrelial C1r inhibitors may differ. To test this, we utilized the crystal structures of the C-terminal domains of BBK32, FbpA, FbpB, and FbpC to carry out 1 micros molecular dynamics simulations, which revealed borrelial C1r inhibitors adopt energetically favored open and closed states defined by two functionally critical regions. This study advances our understanding of how protein dynamics contribute to the function of bacterial immune evasion proteins and reveals a surprising plasticity in the structures of borrelial C1r inhibitors.
-
-	"Conformational dynamics of C1r inhibitor proteins from Lyme disease and relapsing fever spirochetes".,Roy S, Booth CE, Powell-Pierce AD, Schulz AM, Skare JT, Garcia BL bioRxiv. 2023 Mar 1:2023.03.01.530473. doi: 10.1101/2023.03.01.530473. Preprint. PMID:36909632<ref>PMID:36909632</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 8ec3" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 05:39, 7 June 2023

2023-06-07T05:39:38Z

←Older revision		Revision as of 05:39, 7 June 2023
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-	'''Unreleased structure'''

-	The ~~entry~~ 8ec3 is ~~ON HOLD until Paper~~ Publication	+	==The crystal structure of the complement inhibitory domain of Borrelia hermsii FbpC.==
		+	<StructureSection load='8ec3' size='340' side='right'caption='[[8ec3]], [[Resolution\|resolution]] 1.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8ec3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Borrelia_hermsii_HS1 Borrelia hermsii HS1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EC3 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=8ec3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ec3 OCA], [https://pdbe.org/8ec3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ec3 RCSB], [https://www.ebi.ac.uk/pdbsum/8ec3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ec3 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/G9BXS5_BORHE G9BXS5_BORHE]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Borrelial pathogens are vector-borne etiological agents of Lyme disease, relapsing fever, and Borrelia miyamotoi disease. These spirochetes each encode several surface-localized lipoproteins that bind to components of the human complement system. BBK32 is an example of a borrelial lipoprotein that protects the Lyme disease spirochete from complement-mediated attack. The complement inhibitory activity of BBK32 arises from an alpha helical C-terminal domain that interacts directly with the initiating protease of the classical pathway, C1r. Borrelia miyamotoi spirochetes encode BBK32 orthologs termed FbpA and FbpB, and these proteins also inhibit C1r, albeit via distinct recognition mechanisms. The C1r-inhibitory activities of a third ortholog termed FbpC, which is found exclusively in relapsing fever spirochetes, remains unknown. Here we report the crystal structure of the C-terminal domain of B. hermsii FbpC to a limiting resolution of 1.5 A. Surface plasmon resonance studies and assays of complement function demonstrate that FbpC retains potent BBK32-like anti-complement activities. Based on the structure of FbpC, we hypothesized that conformational dynamics of the complement inhibitory domains of borrelial C1r inhibitors may differ. To test this, we utilized the crystal structures of the C-terminal domains of BBK32, FbpA, FbpB, and FbpC to carry out 1 micros molecular dynamics simulations, which revealed borrelial C1r inhibitors adopt energetically favored open and closed states defined by two functionally critical regions. This study advances our understanding of how protein dynamics contribute to the function of bacterial immune evasion proteins and reveals a surprising plasticity in the structures of borrelial C1r inhibitors.

-	~~Authors~~:	+	"Conformational dynamics of C1r inhibitor proteins from Lyme disease and relapsing fever spirochetes".,Roy S, Booth CE, Powell-Pierce AD, Schulz AM, Skare JT, Garcia BL bioRxiv. 2023 Mar 1:2023.03.01.530473. doi: 10.1101/2023.03.01.530473. Preprint. PMID:36909632<ref>PMID:36909632</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 8ec3" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Borrelia hermsii HS1]]
		+	[[Category: Large Structures]]
		+	[[Category: Booth CE]]
		+	[[Category: Garcia BL]]

OCA at 05:47, 14 September 2022

2022-09-14T05:47:04Z

←Older revision		Revision as of 05:47, 14 September 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8ec3 is ON HOLD	+	The entry 8ec3 is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "8ec3" [edit=sysop:move=sysop]

2022-09-07T15:38:30Z

Protected "8ec3" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:38, 7 September 2022

OCA: New page: '''Unreleased structure''' The entry 8ec3 is ON HOLD Authors: Description: Category: Unreleased Structures

2022-09-07T15:38:29Z

New page: '''Unreleased structure''' The entry 8ec3 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 8ec3 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]