6u58 - Revision history

OCA at 14:56, 13 March 2024

OCA — Wed, 13 Mar 2024 14:56:31 GMT

←Older revision		Revision as of 14:56, 13 March 2024
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	<StructureSection load='6u58' size='340' side='right'caption='[[6u58]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='6u58' size='340' side='right'caption='[[6u58]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6u58]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U58 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6U58 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6u58]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6U58 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=SO4:SULFATE+ION'>SO4</scene~~></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Hybrid , Neutron Diffraction , X-ray diffraction, [[Resolution\|Resolution]] 1.9Å</td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6]~~ </~~span~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6u58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u58 OCA], [~~http~~://pdbe.org/6u58 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6u58 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6u58 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6u58 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=6u58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u58 OCA], [https://pdbe.org/6u58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6u58 RCSB], [https://www.ebi.ac.uk/pdbsum/6u58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6u58 ProSAT]</span></td></tr>
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[https://www.uniprot.org/uniprot/BLT1_ECOLX BLT1_ECOLX] Has strong cefotaxime-hydrolyzing activity.
-	The amino-acid sequence of the Toho-1 beta-lactamase contains several conserved residues in the active site, including Ser70, Lys73, Ser130 and Glu166, some of which coordinate a catalytic water molecule. This catalytic water molecule is essential in the acylation and deacylation parts of the reaction mechanism through which Toho-1 inactivates specific antibiotics and provides resistance to its expressing bacterial strains. To investigate the function of Glu166 in the acylation part of the catalytic mechanism, neutron and X-ray crystallographic studies were performed on a Glu166Gln mutant. The structure of this class A beta-lactamase mutant provides several insights into its previously reported reduced drug-binding kinetic rates. A joint refinement of both X-ray and neutron diffraction data was used to study the effects of the Glu166Gln mutation on the active site of Toho-1. This structure reveals that while the Glu166Gln mutation has a somewhat limited impact on the positions of the conserved amino acids within the active site, it displaces the catalytic water molecule from the active site. These subtle changes offer a structural explanation for the previously observed decreases in the binding of non-beta-~~lactam inhibitors such as the recently developed diazobicyclooctane inhibitor avibactam~~.	+

-	Probing the role of the conserved residue Glu166 in a class A beta-lactamase using neutron and X-ray protein crystallography.,Langan PS, Sullivan B, Weiss KL, Coates L Acta Crystallogr D Struct Biol. 2020 Feb 1;76(Pt 2):118-123. doi:, 10.1107/S2059798319016334. Epub 2020 Jan 24. PMID:32038042<ref>PMID:32038042</ref>	+	==See Also==
-		+	*[[Beta-lactamase 3D structures\|Beta-lactamase 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class~~=~~"pdbe-citations 6u58" style~~=~~"background-color:#fffaf0;"></div>~~	+
-	~~== References~~ ==	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Beta-lactamase~~]]	+	[[Category: Escherichia coli]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Langan~~, P S~~]]	+	[[Category: Langan PS]]
-	[[Category: Sullivan, B]]	+	[[Category: Sullivan B]]
-	[[Category: Weiss~~, K L]]~~	+	[[Category: Weiss KL]]
-	~~[[Category: Hydrolase~~]]	+

OCA at 06:41, 19 February 2020

OCA — Wed, 19 Feb 2020 06:41:34 GMT

←Older revision		Revision as of 06:41, 19 February 2020
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-	'''Unreleased structure'''

-	~~The entry~~ 6u58 is ~~ON HOLD until Paper~~ Publication	+	==Toho1 Beta Lactamase Glu166Gln Mutant==
		+	<StructureSection load='6u58' size='340' side='right'caption='[[6u58]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6u58]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U58 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6U58 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </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=6u58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u58 OCA], [http://pdbe.org/6u58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6u58 RCSB], [http://www.ebi.ac.uk/pdbsum/6u58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6u58 ProSAT]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The amino-acid sequence of the Toho-1 beta-lactamase contains several conserved residues in the active site, including Ser70, Lys73, Ser130 and Glu166, some of which coordinate a catalytic water molecule. This catalytic water molecule is essential in the acylation and deacylation parts of the reaction mechanism through which Toho-1 inactivates specific antibiotics and provides resistance to its expressing bacterial strains. To investigate the function of Glu166 in the acylation part of the catalytic mechanism, neutron and X-ray crystallographic studies were performed on a Glu166Gln mutant. The structure of this class A beta-lactamase mutant provides several insights into its previously reported reduced drug-binding kinetic rates. A joint refinement of both X-ray and neutron diffraction data was used to study the effects of the Glu166Gln mutation on the active site of Toho-1. This structure reveals that while the Glu166Gln mutation has a somewhat limited impact on the positions of the conserved amino acids within the active site, it displaces the catalytic water molecule from the active site. These subtle changes offer a structural explanation for the previously observed decreases in the binding of non-beta-lactam inhibitors such as the recently developed diazobicyclooctane inhibitor avibactam.

-	~~Authors~~:	+	Probing the role of the conserved residue Glu166 in a class A beta-lactamase using neutron and X-ray protein crystallography.,Langan PS, Sullivan B, Weiss KL, Coates L Acta Crystallogr D Struct Biol. 2020 Feb 1;76(Pt 2):118-123. doi:, 10.1107/S2059798319016334. Epub 2020 Jan 24. PMID:32038042<ref>PMID:32038042</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 6u58" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Beta-lactamase]]
		+	[[Category: Large Structures]]
		+	[[Category: Langan, P S]]
		+	[[Category: Sullivan, B]]
		+	[[Category: Weiss, K L]]
		+	[[Category: Hydrolase]]

OCA at 06:31, 4 December 2019

OCA — Wed, 04 Dec 2019 06:31:20 GMT

←Older revision		Revision as of 06:31, 4 December 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6u58 is ON HOLD	+	The entry 6u58 is ON HOLD until Paper Publication

	Authors:		Authors:

OCA at 13:44, 20 November 2019

OCA — Wed, 20 Nov 2019 13:44:45 GMT

←Older revision		Revision as of 13:44, 20 November 2019
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6u58 is ON HOLD ~~until sometime in the future~~	+	The entry 6u58 is ON HOLD

	Authors:		Authors:

OCA: Protected "6u58" [edit=sysop:move=sysop]

OCA — Wed, 02 Oct 2019 08:13:50 GMT

Protected "6u58" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:13, 2 October 2019

OCA: New page: '''Unreleased structure''' The entry 6u58 is ON HOLD until sometime in the future Authors: Description: Category: Unreleased Structures

OCA — Wed, 02 Oct 2019 08:13:48 GMT

New page: '''Unreleased structure''' The entry 6u58 is ON HOLD until sometime in the future Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6u58 is ON HOLD until sometime in the future

Authors:

Description:
[[Category: Unreleased Structures]]