6t35 - Revision history

OCA at 10:48, 27 March 2024

OCA — Wed, 27 Mar 2024 10:48:41 GMT

←Older revision		Revision as of 10:48, 27 March 2024
Line 10:		Line 10:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/AMPC_ECOLI AMPC_ECOLI] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.		[https://www.uniprot.org/uniprot/AMPC_ECOLI AMPC_ECOLI] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	SignificanceMicrobial resistance to beta-lactam antibiotics mediated by beta-lactamase-catalyzed hydrolysis is a major global health concern. Penam sulfones, which are structurally related to penicillins, inhibit clinically important serine beta-lactamases (SBLs) by forming transiently stable covalent complexes, thereby protecting beta-lactam antibiotics from hydrolysis. The characterization of these complexes and mechanisms of SBL inhibition is important for development of new SBL inhibitors (SBLi). Studies on the mechanism of the new SBLi enmetazobactam employing mass spectrometry and X-ray crystallography inform on its mode of action and also lead to reevaluation of mechanisms of current clinically important SBLi. In addition to insights into the mechanisms of transient SBL inhibition by penam sulfones, the results reveal potential for penam sulfone optimization to enable irreversible SBL inhibition.
-
-	Studies on enmetazobactam clarify mechanisms of widely used beta-lactamase inhibitors.,Lang PA, Raj R, Tumber A, Lohans CT, Rabe P, Robinson CV, Brem J, Schofield CJ Proc Natl Acad Sci U S A. 2022 May 3;119(18):e2117310119. doi:, 10.1073/pnas.2117310119. Epub 2022 Apr 29. PMID:35486701<ref>PMID:35486701</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 6t35" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Beta-lactamase 3D structures\|Beta-lactamase 3D structures]]		*[[Beta-lactamase 3D structures\|Beta-lactamase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 12:53, 24 January 2024

OCA — Wed, 24 Jan 2024 12:53:41 GMT

←Older revision		Revision as of 12:53, 24 January 2024
Line 1:		Line 1:

	==Crystal structure of AmpC from E.coli with Enmetazobactam (AAI-101)==		==Crystal structure of AmpC from E.coli with Enmetazobactam (AAI-101)==
-	<StructureSection load='6t35' size='340' side='right'caption='[[6t35]]' scene=''>	+	<StructureSection load='6t35' size='340' side='right'caption='[[6t35]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T35 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6t35]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T35 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=6t35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t35 OCA], [https://pdbe.org/6t35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t35 RCSB], [https://www.ebi.ac.uk/pdbsum/6t35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t35 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]] 1.75Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=M9W:Enmetazobactam+derived+trans-enamine+adduct.'>M9W</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6t35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t35 OCA], [https://pdbe.org/6t35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t35 RCSB], [https://www.ebi.ac.uk/pdbsum/6t35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t35 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/AMPC_ECOLI AMPC_ECOLI] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	SignificanceMicrobial resistance to beta-lactam antibiotics mediated by beta-lactamase-catalyzed hydrolysis is a major global health concern. Penam sulfones, which are structurally related to penicillins, inhibit clinically important serine beta-lactamases (SBLs) by forming transiently stable covalent complexes, thereby protecting beta-lactam antibiotics from hydrolysis. The characterization of these complexes and mechanisms of SBL inhibition is important for development of new SBL inhibitors (SBLi). Studies on the mechanism of the new SBLi enmetazobactam employing mass spectrometry and X-ray crystallography inform on its mode of action and also lead to reevaluation of mechanisms of current clinically important SBLi. In addition to insights into the mechanisms of transient SBL inhibition by penam sulfones, the results reveal potential for penam sulfone optimization to enable irreversible SBL inhibition.
		+
		+	Studies on enmetazobactam clarify mechanisms of widely used beta-lactamase inhibitors.,Lang PA, Raj R, Tumber A, Lohans CT, Rabe P, Robinson CV, Brem J, Schofield CJ Proc Natl Acad Sci U S A. 2022 May 3;119(18):e2117310119. doi:, 10.1073/pnas.2117310119. Epub 2022 Apr 29. PMID:35486701<ref>PMID:35486701</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6t35" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Beta-lactamase 3D structures\|Beta-lactamase 3D structures]]		*[[Beta-lactamase 3D structures\|Beta-lactamase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Escherichia coli K-12]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Brem J]]		[[Category: Brem J]]

OCA at 14:42, 31 August 2022

OCA — Wed, 31 Aug 2022 14:42:24 GMT

←Older revision		Revision as of 14:42, 31 August 2022
Line 1:		Line 1:

	==Crystal structure of AmpC from E.coli with Enmetazobactam (AAI-101)==		==Crystal structure of AmpC from E.coli with Enmetazobactam (AAI-101)==
-	<StructureSection load='6t35' size='340' side='right'caption='[[6t35]]~~, [[Resolution\|resolution]] 1.75Å~~' scene=''>	+	<StructureSection load='6t35' size='340' side='right'caption='[[6t35]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>~~[[6t35]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli].~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T35 FirstGlance]. <br>	+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T35 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=M9W:Enmetazobactam+derived+trans-enamine+adduct.'>M9W</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6t35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t35 OCA], [https://pdbe.org/6t35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t35 RCSB], [https://www.ebi.ac.uk/pdbsum/6t35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t35 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ampC, ampA, b4150, JW4111 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=6t35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t35 OCA], [https://pdbe.org/6t35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t35 RCSB], [https://www.ebi.ac.uk/pdbsum/6t35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t35 ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Function ==
-	[[https://www.uniprot.org/uniprot/AMPC_ECOLI AMPC_ECOLI]] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	SignificanceMicrobial resistance to beta-lactam antibiotics mediated by beta-lactamase-catalyzed hydrolysis is a major global health concern. Penam sulfones, which are structurally related to penicillins, inhibit clinically important serine beta-lactamases (SBLs) by forming transiently stable covalent complexes, thereby protecting beta-lactam antibiotics from hydrolysis. The characterization of these complexes and mechanisms of SBL inhibition is important for development of new SBL inhibitors (SBLi). Studies on the mechanism of the new SBLi enmetazobactam employing mass spectrometry and X-ray crystallography inform on its mode of action and also lead to reevaluation of mechanisms of current clinically important SBLi. In addition to insights into the mechanisms of transient SBL inhibition by penam sulfones, the results reveal potential for penam sulfone optimization to enable irreversible SBL inhibition.
-
-	Studies on enmetazobactam clarify mechanisms of widely used beta-lactamase inhibitors.,Lang PA, Raj R, Tumber A, Lohans CT, Rabe P, Robinson CV, Brem J, Schofield CJ Proc Natl Acad Sci U S A. 2022 May 3;119(18):e2117310119. doi:, 10.1073/pnas.2117310119. Epub 2022 Apr 29. PMID:35486701<ref>PMID:35486701</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 6t35" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Beta-lactamase 3D structures\|Beta-lactamase 3D structures]]		*[[Beta-lactamase 3D structures\|Beta-lactamase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Beta-lactamase]]
-	[[Category: Ecoli]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Brem, J]]	+	[[Category: Brem J]]
-	[[Category: Lang~~, P A~~]]	+	[[Category: Lang PA]]
-	[[Category: Leissing~~, T M~~]]	+	[[Category: Leissing TM]]
-	[[Category: Schofield~~, C J]]~~	+	[[Category: Schofield CJ]]
-	~~[[Category: Antibiotic resistance]]~~	+
-	~~[[Category: Antimicrobial protein]]~~	+
-	~~[[Category: Beta lactamase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Mechanism based inhibitor~~]]	+

OCA at 06:23, 12 May 2022

OCA — Thu, 12 May 2022 06:23:22 GMT

←Older revision		Revision as of 06:23, 12 May 2022
Line 1:		Line 1:

	==Crystal structure of AmpC from E.coli with Enmetazobactam (AAI-101)==		==Crystal structure of AmpC from E.coli with Enmetazobactam (AAI-101)==
-	<StructureSection load='6t35' size='340' side='right'caption='[[6t35]]' scene=''>	+	<StructureSection load='6t35' size='340' side='right'caption='[[6t35]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T35 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6T35 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6t35]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T35 FirstGlance]. <br>
-	</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=6t35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t35 OCA], [~~http~~://pdbe.org/6t35 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6t35 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6t35 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6t35 ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=M9W:Enmetazobactam+derived+trans-enamine+adduct.'>M9W</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ampC, ampA, b4150, JW4111 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=6t35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t35 OCA], [https://pdbe.org/6t35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t35 RCSB], [https://www.ebi.ac.uk/pdbsum/6t35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t35 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/AMPC_ECOLI AMPC_ECOLI]] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	SignificanceMicrobial resistance to beta-lactam antibiotics mediated by beta-lactamase-catalyzed hydrolysis is a major global health concern. Penam sulfones, which are structurally related to penicillins, inhibit clinically important serine beta-lactamases (SBLs) by forming transiently stable covalent complexes, thereby protecting beta-lactam antibiotics from hydrolysis. The characterization of these complexes and mechanisms of SBL inhibition is important for development of new SBL inhibitors (SBLi). Studies on the mechanism of the new SBLi enmetazobactam employing mass spectrometry and X-ray crystallography inform on its mode of action and also lead to reevaluation of mechanisms of current clinically important SBLi. In addition to insights into the mechanisms of transient SBL inhibition by penam sulfones, the results reveal potential for penam sulfone optimization to enable irreversible SBL inhibition.
		+
		+	Studies on enmetazobactam clarify mechanisms of widely used beta-lactamase inhibitors.,Lang PA, Raj R, Tumber A, Lohans CT, Rabe P, Robinson CV, Brem J, Schofield CJ Proc Natl Acad Sci U S A. 2022 May 3;119(18):e2117310119. doi:, 10.1073/pnas.2117310119. Epub 2022 Apr 29. PMID:35486701<ref>PMID:35486701</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6t35" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Beta-lactamase 3D structures\|Beta-lactamase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Beta-lactamase]]
		+	[[Category: Ecoli]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Brem J]]	+	[[Category: Brem, J]]
-	[[Category: Lang PA]]	+	[[Category: Lang, P A]]
-	[[Category: Leissing TM]]	+	[[Category: Leissing, T M]]
-	[[Category: Schofield CJ]]	+	[[Category: Schofield, C J]]
		+	[[Category: Antibiotic resistance]]
		+	[[Category: Antimicrobial protein]]
		+	[[Category: Beta lactamase]]
		+	[[Category: Hydrolase]]
		+	[[Category: Mechanism based inhibitor]]

OCA at 09:33, 18 November 2020

OCA — Wed, 18 Nov 2020 09:33:00 GMT

←Older revision		Revision as of 09:33, 18 November 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6t35 is ~~ON HOLD until Oct 10 2021~~	+	==Crystal structure of AmpC from E.coli with Enmetazobactam (AAI-101)==
-		+	<StructureSection load='6t35' size='340' side='right'caption='[[6t35]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T35 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6T35 FirstGlance]. <br>
-	~~Description~~:	+	</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=6t35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t35 OCA], [http://pdbe.org/6t35 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t35 RCSB], [http://www.ebi.ac.uk/pdbsum/6t35 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t35 ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Brem J]]
		+	[[Category: Lang PA]]
		+	[[Category: Leissing TM]]
		+	[[Category: Schofield CJ]]

OCA at 04:56, 23 October 2019

OCA — Wed, 23 Oct 2019 04:56:42 GMT

←Older revision		Revision as of 04:56, 23 October 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6t35 is ON HOLD	+	The entry 6t35 is ON HOLD until Oct 10 2021

	Authors:		Authors:

OCA: Protected "6t35" [edit=sysop:move=sysop]

OCA — Wed, 16 Oct 2019 04:31:02 GMT

Protected "6t35" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:31, 16 October 2019

OCA: New page: '''Unreleased structure''' The entry 6t35 is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 16 Oct 2019 04:31:00 GMT

New page: '''Unreleased structure''' The entry 6t35 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6t35 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]