1x7u - Revision history

OCA: Redirecting to 5l02

2016-08-10T15:31:20Z

Redirecting to 5l02

←Older revision		Revision as of 15:31, 10 August 2016
Line 1:		Line 1:
-	~~==Crystal structure of the S324T of catalase-peroxidase KatG==~~	+	#REDIRECT [[5l02]] This PDB entry is obsolete and replaced by 5l02
-	~~<StructureSection load='1x7u' size='340' side='right' caption='~~[[~~1x7u]], [[Resolution\|resolution]] 1.90Å' scene=''>~~	+
-	~~== Structural highlights ==~~	+
-	~~<table><tr><td colspan='2'>[[1x7u~~]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pseudomallei"_whitmore_1913 "bacillus pseudomallei" whitmore 1913]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X7U FirstGlance]. <br>	+
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>	+
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mwv\|1mwv]]</td></tr>~~	+
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KatG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28450 "Bacillus pseudomallei" Whitmore 1913])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </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=1x7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x7u OCA], [http://pdbe.org/1x7u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x7u RCSB], [http://www.ebi.ac.uk/pdbsum/1x7u PDBsum]</span></td></tr>	+
-	~~</table>~~	+
-	~~== Function ==~~	+
-	~~[[http://www.uniprot.org/uniprot/KATG_BURPS KATG_BURPS]] Bifunctional enzyme with both catalase~~ and ~~broad-spectrum peroxidase activity. Displays also NADH oxidase, isoniazid hydrazine lyase and isonicotinoyl-NAD synthase activity.<ref>PMID:15280362</ref>~~	+
-	~~== Evolutionary Conservation ==~~	+
-	~~[[Image:Consurf_key_small.gif\|200px\|right]]~~	+
-	~~Check<jmol>~~	+
-	~~<jmolCheckbox>~~	+
-	~~<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x7/1x7u_consurf.spt"</scriptWhenChecked>~~	+
-	~~<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>~~	+
-	~~<text>to colour the structure~~ by ~~Evolutionary Conservation</text>~~	+
-	~~</jmolCheckbox>~~	+
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1x7u ConSurf].	+
-	~~<div style="clear:both"></div>~~	+
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The Ser315Thr variant of the catalase-peroxidase KatG from Mycobacterium tuberculosis imparts resistance to the pro-drug isonicotinic acid hydrazide (isoniazid) through a failure to convert it to the active drug, isonicotinoyl-NAD. The equivalent variant in KatG from Burkholderia pseudomallei, Ser324Thr, has been constructed, revealing catalase and peroxidase activities that are similar to those of the native enzyme. The other activities of the variant protein, including the NADH oxidase, the isoniazid hydrazinolysis and isonicotinoyl-NAD synthase activities are reduced by 60-70%. The crystal structure of the variant differs from that of the native enzyme in having the methyl group of Thr324 situated in the entrance channel to the heme cavity, in a modified water matrix in the entrance channel and heme cavity, in lacking the putative perhydroxy modification on the heme, in the multiple locations of a few side-chains, and in the presence of an apparent perhydroxy modification on the indole nitrogen atom of the active-site Trp111. The position of the methyl group of Thr324 creates a constriction or narrowing of the channel leading to the heme cavity, providing an explanation for the lower reactivity towards isoniazid and the slower rate of isonicotinoyl-NAD synthesis.	+
-		+
-	Structural characterization of the Ser324Thr variant of the catalase-peroxidase (KatG) from Burkholderia pseudomallei.,Deemagarn T, Carpena X, Singh R, Wiseman B, Fita I, Loewen PC J Mol Biol. 2005 Jan 7;345(1):21-8. PMID:15567407<ref>PMID:15567407</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 1x7u" style="background-color:#fffaf0;"></div>~~	+
-		+
-	~~==See Also==~~	+
-	*[[Catalase\|Catalase]]	+
-	~~== References ==~~	+
-	~~<references/>~~	+
-	~~__TOC__~~	+
-	~~</StructureSection>~~	+
-	~~[[Category: Bacillus pseudomallei whitmore 1913]]~~	+
-	~~[[Category: Catalase]]~~	+
-	~~[[Category: Carpena, X]]~~	+
-	~~[[Category: Deemagarn, T]]~~	+
-	~~[[Category: Fita, I]]~~	+
-	~~[[Category: Loewen, P C]]~~	+
-	~~[[Category: Singh, R]]~~	+
-	~~[[Category: Wiseman, B]]~~	+
-	~~[[Category: Catalase-peroxidase]]~~	+
-	~~[[Category: Inh resistant variant]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+

OCA at 21:55, 7 February 2016

2016-02-07T21:55:44Z

←Older revision		Revision as of 21:55, 7 February 2016
Line 19:		Line 19:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1x7u ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 05:17, 10 September 2015

2015-09-10T05:17:48Z

←Older revision		Revision as of 05:17, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1x7u' size='340' side='right' caption='[[1x7u]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1x7u' size='340' side='right' caption='[[1x7u]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1x7u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Burkholderia_pseudomallei Burkholderia~~ pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X7U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1x7u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pseudomallei"_whitmore_1913 "bacillus pseudomallei" whitmore 1913]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X7U FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mwv\|1mwv]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mwv\|1mwv]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KatG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28450 ~~Burkholderia~~ pseudomallei])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KatG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28450 "Bacillus pseudomallei" Whitmore 1913])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </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=1x7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x7u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1x7u RCSB], [http://www.ebi.ac.uk/pdbsum/1x7u 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=1x7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x7u OCA], [http://pdbe.org/1x7u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x7u RCSB], [http://www.ebi.ac.uk/pdbsum/1x7u PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/KATG_BURPS KATG_BURPS]] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, isoniazid hydrazine lyase and isonicotinoyl-NAD synthase activity.<ref>PMID:15280362</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 27:		Line 29:
	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 1x7u" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Burkholderia~~ pseudomallei]]	+	[[Category: Bacillus pseudomallei whitmore 1913]]
	[[Category: Catalase]]		[[Category: Catalase]]
	[[Category: Carpena, X]]		[[Category: Carpena, X]]

OCA at 14:09, 6 January 2015

2015-01-06T14:09:57Z

←Older revision		Revision as of 14:09, 6 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1x7u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X7U FirstGlance]. <br>		<table><tr><td colspan='2'>[[1x7u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X7U FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mwv\|1mwv]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mwv\|1mwv]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KatG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28450 Burkholderia pseudomallei])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KatG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28450 Burkholderia pseudomallei])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x7u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1x7u RCSB], [http://www.ebi.ac.uk/pdbsum/1x7u 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=1x7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x7u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1x7u RCSB], [http://www.ebi.ac.uk/pdbsum/1x7u PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 36:
	[[Category: Burkholderia pseudomallei]]		[[Category: Burkholderia pseudomallei]]
	[[Category: Catalase]]		[[Category: Catalase]]
-	[[Category: Carpena, X.]]	+	[[Category: Carpena, X]]
-	[[Category: Deemagarn, T.]]	+	[[Category: Deemagarn, T]]
-	[[Category: Fita, I.]]	+	[[Category: Fita, I]]
-	[[Category: Loewen, P C.]]	+	[[Category: Loewen, P C]]
-	[[Category: Singh, R.]]	+	[[Category: Singh, R]]
-	[[Category: Wiseman, B.]]	+	[[Category: Wiseman, B]]
	[[Category: Catalase-peroxidase]]		[[Category: Catalase-peroxidase]]
	[[Category: Inh resistant variant]]		[[Category: Inh resistant variant]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 20:43, 28 September 2014

2014-09-28T20:43:52Z

←Older revision		Revision as of 20:43, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1x7u.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of the S324T of catalase-peroxidase KatG==
		+	<StructureSection load='1x7u' size='340' side='right' caption='[[1x7u]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1x7u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X7U FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mwv\|1mwv]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KatG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28450 Burkholderia pseudomallei])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x7u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1x7u RCSB], [http://www.ebi.ac.uk/pdbsum/1x7u PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x7/1x7u_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The Ser315Thr variant of the catalase-peroxidase KatG from Mycobacterium tuberculosis imparts resistance to the pro-drug isonicotinic acid hydrazide (isoniazid) through a failure to convert it to the active drug, isonicotinoyl-NAD. The equivalent variant in KatG from Burkholderia pseudomallei, Ser324Thr, has been constructed, revealing catalase and peroxidase activities that are similar to those of the native enzyme. The other activities of the variant protein, including the NADH oxidase, the isoniazid hydrazinolysis and isonicotinoyl-NAD synthase activities are reduced by 60-70%. The crystal structure of the variant differs from that of the native enzyme in having the methyl group of Thr324 situated in the entrance channel to the heme cavity, in a modified water matrix in the entrance channel and heme cavity, in lacking the putative perhydroxy modification on the heme, in the multiple locations of a few side-chains, and in the presence of an apparent perhydroxy modification on the indole nitrogen atom of the active-site Trp111. The position of the methyl group of Thr324 creates a constriction or narrowing of the channel leading to the heme cavity, providing an explanation for the lower reactivity towards isoniazid and the slower rate of isonicotinoyl-NAD synthesis.

-	~~{{STRUCTURE_1x7u\| PDB=1x7u \| SCENE= }}~~	+	Structural characterization of the Ser324Thr variant of the catalase-peroxidase (KatG) from Burkholderia pseudomallei.,Deemagarn T, Carpena X, Singh R, Wiseman B, Fita I, Loewen PC J Mol Biol. 2005 Jan 7;345(1):21-8. PMID:15567407<ref>PMID:15567407</ref>

-	~~===Crystal structure~~ of the ~~S324T of catalase-peroxidase KatG===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_15567407}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1x7u]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1X7U OCA].~~	+

	==See Also==		==See Also==
	*[[Catalase\|Catalase]]		*[[Catalase\|Catalase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:015567407<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Burkholderia pseudomallei]]		[[Category: Burkholderia pseudomallei]]
	[[Category: Catalase]]		[[Category: Catalase]]

OCA at 07:58, 20 October 2012

2012-10-20T07:58:25Z

←Older revision		Revision as of 07:58, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1x7u]] is a 2 chain structure ~~of [[Catalase]]~~ with sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X7U OCA].	+	[[1x7u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X7U OCA].

	==See Also==		==See Also==

OCA: Protected "1x7u" [edit=sysop:move=sysop]

2012-07-25T18:02:43Z

Protected "1x7u" [edit=sysop:move=sysop]

←Older revision

Revision as of 18:02, 25 July 2012

OCA at 18:02, 25 July 2012

2012-07-25T18:02:42Z

←Older revision		Revision as of 18:02, 25 July 2012
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-	{{Seed}}
	[[Image:1x7u.png\|left\|200px]]		[[Image:1x7u.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_1x7u\| PDB=1x7u \| SCENE= }}		{{STRUCTURE_1x7u\| PDB=1x7u \| SCENE= }}

	===Crystal structure of the S324T of catalase-peroxidase KatG===		===Crystal structure of the S324T of catalase-peroxidase KatG===

-
-	<!--
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	{{ABSTRACT_PUBMED_15567407}}		{{ABSTRACT_PUBMED_15567407}}

	==About this Structure==		==About this Structure==
-	~~1X7U~~ is a 2 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X7U OCA].	+	[[1x7u]] is a 2 chain structure of [[Catalase]] with sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X7U OCA].
		+
		+	==See Also==
		+	*[[Catalase\|Catalase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~15567407~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:015567407</ref><references group="xtra"/>
	[[Category: Burkholderia pseudomallei]]		[[Category: Burkholderia pseudomallei]]
	[[Category: Catalase]]		[[Category: Catalase]]
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	[[Category: Catalase-peroxidase]]		[[Category: Catalase-peroxidase]]
	[[Category: Inh resistant variant]]		[[Category: Inh resistant variant]]
-		+	[[Category: Oxidoreductase]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Mon Feb 16 16:45:42 2009''~~	+

OCA at 14:45, 16 February 2009

2009-02-16T14:45:43Z

←Older revision		Revision as of 14:45, 16 February 2009
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	==About this Structure==		==About this Structure==
-	1X7U is a ~~[[Single protein]]~~ structure of ~~sequence~~ from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X7U OCA].	+	1X7U is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X7U OCA].

	==Reference==		==Reference==
-	Structural characterization of the Ser324Thr variant of the catalase-peroxidase (KatG) from Burkholderia pseudomallei., Deemagarn T, Carpena X, Singh R, Wiseman B, Fita I, Loewen PC, J Mol Biol. 2005 Jan 7;345(1):21-8. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/15567407 15567407]~~	+	<ref group="xtra">PMID:15567407</ref><references group="xtra"/>
	[[Category: Burkholderia pseudomallei]]		[[Category: Burkholderia pseudomallei]]
	[[Category: Catalase]]		[[Category: Catalase]]
-	[[Category: Single protein]]
	[[Category: Carpena, X.]]		[[Category: Carpena, X.]]
	[[Category: Deemagarn, T.]]		[[Category: Deemagarn, T.]]
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	[[Category: Inh resistant variant]]		[[Category: Inh resistant variant]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun Jul 27 20~~:00:~~27 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 16:45:42 2009''

OCA at 17:00, 27 July 2008

2008-07-27T17:00:29Z

←Older revision		Revision as of 17:00, 27 July 2008
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-	[[Image:1x7u.~~jpg~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:1x7u.png\|left\|200px]]

	<!--		<!--
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	{{STRUCTURE_1x7u\| PDB=1x7u \| SCENE= }}		{{STRUCTURE_1x7u\| PDB=1x7u \| SCENE= }}

-	~~'''~~Crystal structure of the S324T of catalase-peroxidase KatG~~'''~~	+	===Crystal structure of the S324T of catalase-peroxidase KatG===


-	~~==Overview==~~	+	<!--
-	The ~~Ser315Thr variant of~~ the ~~catalase-peroxidase KatG from Mycobacterium tuberculosis imparts resistance~~ to the ~~pro-drug isonicotinic acid hydrazide~~ (~~isoniazid) through a failure to convert~~ it ~~to the active drug, isonicotinoyl-NAD~~. ~~The equivalent variant in KatG from Burkholderia pseudomallei, Ser324Thr, has been constructed, revealing catalase and peroxidase activities that are similar to those of the native enzyme~~. ~~The other activities of the variant protein~~, ~~including~~ the ~~NADH oxidase, the isoniazid hydrazinolysis and isonicotinoyl-NAD synthase activities are reduced by 60-70%~~. The crystal structure of the variant differs from that of the native enzyme in having the methyl group of Thr324 situated in the entrance channel to the heme cavity, in a modified water matrix in the entrance channel and heme cavity, in lacking the putative perhydroxy modification on the heme, in the multiple locations of a few side-~~chains, and in the presence of an apparent perhydroxy modification on the indole nitrogen atom of the active~~-site Trp111. The position of the methyl group of Thr324 creates a constriction or narrowing of the channel leading to the heme cavity, providing an explanation for the lower reactivity towards isoniazid and the slower rate of isonicotinoyl-NAD synthesis.	+	The line below this paragraph, {{ABSTRACT_PUBMED_15567407}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 15567407 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_15567407}}

	==About this Structure==		==About this Structure==
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	[[Category: Catalase-peroxidase]]		[[Category: Catalase-peroxidase]]
	[[Category: Inh resistant variant]]		[[Category: Inh resistant variant]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 14~~:40:48 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:00:27 2008''