4ibr - Revision history

OCA at 15:19, 20 September 2023

2023-09-20T15:19:47Z

←Older revision		Revision as of 15:19, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ibr]] 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=4IBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IBR FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ibr]] 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=4IBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IBR FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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]] 2.2Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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=4ibr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ibr OCA], [https://pdbe.org/4ibr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ibr RCSB], [https://www.ebi.ac.uk/pdbsum/4ibr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ibr 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=4ibr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ibr OCA], [https://pdbe.org/4ibr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ibr RCSB], [https://www.ebi.ac.uk/pdbsum/4ibr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ibr ProSAT]</span></td></tr>
	</table>		</table>

OCA at 08:57, 9 November 2022

2022-11-09T08:57:34Z

←Older revision		Revision as of 08:57, 9 November 2022
Line 1:		Line 1:

	==Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying G238S/E104K mutations==		==Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying G238S/E104K mutations==
-	<StructureSection load='4ibr' size='340' side='right' caption='[[4ibr]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='4ibr' size='340' side='right'caption='[[4ibr]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ibr]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"bacillus_coli"_migula_1895 "bacillus~~ coli~~" migula 1895~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IBR OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4IBR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ibr]] 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=4IBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IBR FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l7u\|1l7u]], [[1ero\|1ero]], [[4ibx\|4ibx]]</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=4ibr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ibr OCA], [https://pdbe.org/4ibr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ibr RCSB], [https://www.ebi.ac.uk/pdbsum/4ibr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ibr ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">bla-TEM-94 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=4ibr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ibr OCA], [~~http~~://pdbe.org/4ibr PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ibr RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ibr PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ibr ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/BLAT_ECOLX BLAT_ECOLX]] TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8/CAZ-2, TEM-16/CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta-lactamase inhibitors.	+	[https://www.uniprot.org/uniprot/BLAT_ECOLX BLAT_ECOLX] TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8/CAZ-2, TEM-16/CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta-lactamase inhibitors.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4ibr" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4ibr" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Beta-lactamase 3D structures\|Beta-lactamase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus~~ coli ~~migula 1895~~]]	+	[[Category: Escherichia coli]]
-	[[Category: ~~Beta-lactamase~~]]	+	[[Category: Large Structures]]
-	[[Category: Dellus-Gur, E]]	+	[[Category: Dellus-Gur E]]
-	[[Category: Elias, M]]	+	[[Category: Elias M]]
-	[[Category: Tawfik~~, D S~~]]	+	[[Category: Tawfik DS]]
-	[[Category: Toth-Petroczy, A]]	+	[[Category: Toth-Petroczy A]]
-	~~[[Category: Hydrolase~~]]	+

OCA at 08:52, 15 November 2017

2017-11-15T08:52:47Z

←Older revision		Revision as of 08:52, 15 November 2017
Line 21:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 4ibr" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4ibr" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Beta-lactamase\|Beta-lactamase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:35, 4 August 2016

2016-08-04T17:35:59Z

←Older revision		Revision as of 17:35, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying G238S/E104K mutations==		==Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying G238S/E104K mutations==
	<StructureSection load='4ibr' size='340' side='right' caption='[[4ibr]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='4ibr' size='340' side='right' caption='[[4ibr]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ibr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Gracixalus_waza Gracixalus waza~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IBR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IBR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ibr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IBR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IBR FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l7u\|1l7u]], [[1ero\|1ero]], [[4ibx\|4ibx]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l7u\|1l7u]], [[1ero\|1ero]], [[4ibx\|4ibx]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">bla-TEM-94 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=~~1322172 Gracixalus waza~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">bla-TEM-94 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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='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=4ibr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ibr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ibr RCSB], [http://www.ebi.ac.uk/pdbsum/4ibr PDBsum]</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=4ibr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ibr OCA], [http://pdbe.org/4ibr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ibr RCSB], [http://www.ebi.ac.uk/pdbsum/4ibr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ibr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	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 4ibr" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 26:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Bacillus coli migula 1895]]
	[[Category: Beta-lactamase]]		[[Category: Beta-lactamase]]
-	[[Category: Gracixalus waza]]
	[[Category: Dellus-Gur, E]]		[[Category: Dellus-Gur, E]]
	[[Category: Elias, M]]		[[Category: Elias, M]]

OCA at 17:40, 24 December 2014

2014-12-24T17:40:35Z

←Older revision		Revision as of 17:40, 24 December 2014
Line 9:		Line 9:
	<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=4ibr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ibr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ibr RCSB], [http://www.ebi.ac.uk/pdbsum/4ibr PDBsum]</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=4ibr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ibr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ibr RCSB], [http://www.ebi.ac.uk/pdbsum/4ibr PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/BLAT_ECOLX BLAT_ECOLX]] TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8/CAZ-2, TEM-16/CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta-lactamase inhibitors.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 12:52, 21 December 2014

2014-12-21T12:52:05Z

←Older revision		Revision as of 12:52, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4ibr\| PDB=4ibr \| SCENE= }}~~	+	==Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying G238S/E104K mutations==
-	===Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying G238S/E104K mutations===	+	<StructureSection load='4ibr' size='340' side='right' caption='[[4ibr]], [[Resolution\|resolution]] 2.20Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23542341}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4ibr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gracixalus_waza Gracixalus waza]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IBR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IBR FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l7u\|1l7u]], [[1ero\|1ero]], [[4ibx\|4ibx]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">bla-TEM-94 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1322172 Gracixalus waza])</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=4ibr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ibr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ibr RCSB], [http://www.ebi.ac.uk/pdbsum/4ibr PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Protein evolvability includes two elements-robustness (or neutrality, mutations having no effect) and innovability (mutations readily inducing new functions). How are these two conflicting demands bridged? Does the ability to bridge them relate to the observation that certain folds, such as TIM barrels, accommodate numerous functions, whereas other folds support only one? Here, we hypothesize that the key to innovability is polarity-an active site composed of flexible, loosely packed loops alongside a well-separated, highly ordered scaffold. We show that highly stabilized variants of TEM-1 beta-lactamase exhibit selective rigidification of the enzyme's scaffold while the active-site loops maintained their conformational plasticity. Polarity therefore results in stabilizing, compensatory mutations not trading off, but instead promoting the acquisition of new activities. Indeed, computational analysis indicates that in folds that accommodate only one function throughout evolution, for example, dihydrofolate reductase, >/=60% of the active-site residues belong to the scaffold. In contrast, folds associated with multiple functions such as the TIM barrel show high scaffold-active-site polarity (~20% of the active site comprises scaffold residues) and >2-fold higher rates of sequence divergence at active-site positions. Our work suggests structural measures of fold polarity that appear to be correlated with innovability, thereby providing new insights regarding protein evolution, design, and engineering.

-	~~==Function==~~	+	What Makes a Protein Fold Amenable to Functional Innovation? Fold Polarity and Stability Trade-offs.,Dellus-Gur E, Toth-Petroczy A, Elias M, Tawfik DS J Mol Biol. 2013 Mar 28. pii: S0022-2836(13)00200-3. doi:, 10.1016/j.jmb.2013.03.033. PMID:23542341<ref>PMID:23542341</ref>
-	[[http://www.uniprot.org/uniprot/BLAT_ECOLX BLAT_ECOLX]] TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to ~~penicillins~~ and ~~cephalosporins~~. ~~TEM~~-~~3 and TEM~~-~~4 are capable of hydrolyzing cefotaxime and ceftazidime~~. ~~TEM-5 is capable of hydrolyzing ceftazidime~~. ~~TEM~~-~~6 is capable of hydrolyzing ceftazidime and aztreonam~~. ~~TEM-8/CAZ-2~~, ~~TEM-16~~/~~CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime~~. ~~IRT-4 shows resistance to beta-lactamase inhibitors~~.	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4ibr]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Gracixalus_waza Gracixalus waza]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4IBR OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:023542341</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Beta-lactamase\|Beta-lactamase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Beta-lactamase]]		[[Category: Beta-lactamase]]
	[[Category: Gracixalus waza]]		[[Category: Gracixalus waza]]
-	[[Category: Dellus-Gur, E.]]	+	[[Category: Dellus-Gur, E]]
-	[[Category: Elias, M.]]	+	[[Category: Elias, M]]
-	[[Category: Tawfik, D S.]]	+	[[Category: Tawfik, D S]]
-	[[Category: Toth-Petroczy, A~~.]]~~	+	[[Category: Toth-Petroczy, A]]
-	~~[[Category: Beta-lactamase~~]]	+
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 04:25, 18 July 2013

2013-07-18T04:25:24Z

←Older revision		Revision as of 04:25, 18 July 2013
Line 7:		Line 7:

	==About this Structure==		==About this Structure==
-	[[4ibr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli Escherichia coli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IBR OCA].	+	[[4ibr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gracixalus_waza Gracixalus waza]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IBR OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:023542341</ref><references group="xtra"/><references/>
	[[Category: Beta-lactamase]]		[[Category: Beta-lactamase]]
-	[[Category: ~~Escherichia coli~~]]	+	[[Category: Gracixalus waza]]
	[[Category: Dellus-Gur, E.]]		[[Category: Dellus-Gur, E.]]
	[[Category: Elias, M.]]		[[Category: Elias, M.]]

OCA at 19:27, 17 April 2013

2013-04-17T19:27:04Z

←Older revision		Revision as of 19:27, 17 April 2013
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	{{STRUCTURE_4ibr\| PDB=4ibr \| SCENE= }}		{{STRUCTURE_4ibr\| PDB=4ibr \| SCENE= }}
	===Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying G238S/E104K mutations===		===Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying G238S/E104K mutations===
		+	{{ABSTRACT_PUBMED_23542341}}

	==Function==		==Function==

OCA at 01:49, 4 April 2013

2013-04-04T01:49:51Z

←Older revision		Revision as of 01:49, 4 April 2013
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-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4ibr\| PDB=4ibr \| SCENE= }}
		+	===Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying G238S/E104K mutations===

-	~~The entry 4ibr~~ is ~~ON HOLD until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/BLAT_ECOLX BLAT_ECOLX]] TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8/CAZ-2, TEM-16/CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta-lactamase inhibitors.

-	~~Authors~~: Dellus-Gur, E.~~, Toth-Petroczy, A.,~~ Elias, M., Tawfik, D.S.	+	==About this Structure==
-		+	[[4ibr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IBR OCA].
-	~~Description~~: ~~Crystal structure of stabilized TEM-1 beta~~-lactamase ~~variant v.13 carrying G238S/E104K mutations~~	+	[[Category: Beta-lactamase]]
		+	[[Category: Escherichia coli]]
		+	[[Category: Dellus-Gur, E.]]
		+	[[Category: Elias, M.]]
		+	[[Category: Tawfik, D S.]]
		+	[[Category: Toth-Petroczy, A.]]
		+	[[Category: Beta-lactamase]]
		+	[[Category: Hydrolase]]

OCA at 11:09, 23 January 2013

2013-01-23T11:09:05Z

←Older revision		Revision as of 11:09, 23 January 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4ibr is ON HOLD	+	The entry 4ibr is ON HOLD until Paper Publication

	Authors: Dellus-Gur, E., Toth-Petroczy, A., Elias, M., Tawfik, D.S.		Authors: Dellus-Gur, E., Toth-Petroczy, A., Elias, M., Tawfik, D.S.

	Description: Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying G238S/E104K mutations		Description: Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying G238S/E104K mutations