4dmo - Revision history

OCA at 14:39, 14 March 2024

2024-03-14T14:39:17Z

← Older revision		Revision as of 14:39, 14 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4dmo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DMO FirstGlance]. <br>		<table><tr><td colspan='2'>[[4dmo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DMO FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KH2:3-(1-METHYLPIPERIDINIUM-1-YL)PROPANE-1-SULFONATE'>KH2</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]] 2.14Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KH2:3-(1-METHYLPIPERIDINIUM-1-YL)PROPANE-1-SULFONATE'>KH2</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=4dmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dmo OCA], [https://pdbe.org/4dmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dmo RCSB], [https://www.ebi.ac.uk/pdbsum/4dmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dmo 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=4dmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dmo OCA], [https://pdbe.org/4dmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dmo RCSB], [https://www.ebi.ac.uk/pdbsum/4dmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dmo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/Q81AS3_BACCR Q81AS3_BACCR]]		[https://www.uniprot.org/uniprot/Q81AS3_BACCR Q81AS3_BACCR]
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Arylamine N-acetyltransferases (NAT), a class of xenobiotic-metabolizing enzymes, catalyze the acetylation of aromatic amine compounds through a strictly conserved Cys-His-Asp catalytic triad. Each residue is essential for catalysis in both prokaryotic and eukaryotic NATs. Indeed, in (HUMAN)NAT2 variants, mutation of the Asp residue to Asn, Gln, or Glu dramatically impairs enzyme activity. However, a putative atypical NAT harboring a catalytic triad Glu residue was recently identified in Bacillus cereus [(BACCR)NAT3], but has not yet been characterized. We report here the crystal structure and functional characterization of this atypical NAT. The overall fold of (BACCR)NAT3 and the geometry of its Cys-His-Glu catalytic triad are similar to those present in functional NATs. Importantly, the enzyme was found to be active and to acetylate prototypic arylamine NAT substrates. In contrast to human NAT2, the presence of a Glu or Asp in the triad of (BACCR)NAT3 did not significantly affect enzyme structure or function. Computational analysis identified differences in residue packing and steric constraints in the active site of (BACCR)NAT3 that allow it to accommodate a Cys-His-Glu triad. These findings overturn the conventional view, demonstrating that the catalytic triad of this family of acetyltransferases is plastic. Moreover, they highlight the need for further study of the evolutionary history of NATs and the functional significance of the predominant Cys-His-Asp triad in both prokaryotic and eukaryotic forms.

	Structural and biochemical characterization of an active arylamine N-acetyltransferase possessing a non-canonical Cys-His-Glu catalytic triad.,Kubiak X, de la Sierra-Gallay IL, Chaffotte AF, Pluvinage B, Weber P, Haouz A, Dupret JM, Rodrigues-Lima F J Biol Chem. 2013 Jun 19. PMID:23770703<ref>PMID:23770703</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4dmo" style="background-color:#fffaf0;"></div>~~
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:28, 21 September 2022

2022-09-21T08:28:32Z

← Older revision		Revision as of 08:28, 21 September 2022
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	<StructureSection load='4dmo' size='340' side='right'caption='[[4dmo]], [[Resolution\|resolution]] 2.14Å' scene=''>		<StructureSection load='4dmo' size='340' side='right'caption='[[4dmo]], [[Resolution\|resolution]] 2.14Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4dmo]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Baccr Baccr~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DMO OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4DMO FirstGlance]. <br>		<table><tr><td colspan='2'>[[4dmo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DMO FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KH2:3-(1-METHYLPIPERIDINIUM-1-YL)PROPANE-1-SULFONATE'>KH2</scene~~></td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KH2:3-(1-METHYLPIPERIDINIUM-1-YL)PROPANE-1-SULFONATE'>KH2</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BC_3483, NAT3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=226900 BACCR])</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=4dmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dmo OCA], [https://pdbe.org/4dmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dmo RCSB], [https://www.ebi.ac.uk/pdbsum/4dmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dmo ProSAT]</span></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-hydroxyarylamine_O-acetyltransferase N-hydroxyarylamine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.118 2.3.1.118] </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=4dmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dmo OCA], [~~http~~://pdbe.org/4dmo PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4dmo RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4dmo PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4dmo ProSAT]</span></td></tr>
	</table>		</table>
			== Function ==
			[[https://www.uniprot.org/uniprot/Q81AS3_BACCR Q81AS3_BACCR]]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Baccr~~]]		[[Category: Bacillus cereus ATCC 14579]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	~~[[Category: N-hydroxyarylamine O-acetyltransferase]]~~		[[Category: Haouz A]]
	[[Category: Haouz, A]]		[[Category: Kubiak X]]
	[[Category: Kubiak, X]]		[[Category: Li de la Sierra-Gallay I]]
	[[Category: ~~Rodrigues~~-~~Lima, F~~]]		[[Category: Rodrigues-Lima F]]
	[[Category: ~~Sierra~~-~~Gallay, I Li de la~~]]		[[Category: Weber P]]
	[[Category: Weber, P]]
	~~[[Category: Acetyltransferase]]~~
	~~[[Category: Transferase~~]]

OCA at 11:50, 17 July 2019

2019-07-17T11:50:44Z

← Older revision		Revision as of 11:50, 17 July 2019
Line 1:		Line 1:

	==Crystal structure of the (BACCR)NAT3 arylamine N-acetyltransferase from Bacillus cereus reveals a unique Cys-His-Glu catalytic triad==		==Crystal structure of the (BACCR)NAT3 arylamine N-acetyltransferase from Bacillus cereus reveals a unique Cys-His-Glu catalytic triad==
	<StructureSection load='4dmo' size='340' side='right' caption='[[4dmo]], [[Resolution\|resolution]] 2.14Å' scene=''>		<StructureSection load='4dmo' size='340' side='right'caption='[[4dmo]], [[Resolution\|resolution]] 2.14Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4dmo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baccr Baccr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DMO FirstGlance]. <br>		<table><tr><td colspan='2'>[[4dmo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baccr Baccr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DMO FirstGlance]. <br>
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Baccr]]		[[Category: Baccr]]
			[[Category: Large Structures]]
	[[Category: N-hydroxyarylamine O-acetyltransferase]]		[[Category: N-hydroxyarylamine O-acetyltransferase]]
	[[Category: Haouz, A]]		[[Category: Haouz, A]]

OCA at 02:42, 5 August 2016

2016-08-05T02:42:03Z

← Older revision		Revision as of 02:42, 5 August 2016
Line 1:		Line 1:

	==Crystal structure of the (BACCR)NAT3 arylamine N-acetyltransferase from Bacillus cereus reveals a unique Cys-His-Glu catalytic triad==		==Crystal structure of the (BACCR)NAT3 arylamine N-acetyltransferase from Bacillus cereus reveals a unique Cys-His-Glu catalytic triad==
	<StructureSection load='4dmo' size='340' side='right' caption='[[4dmo]], [[Resolution\|resolution]] 2.14Å' scene=''>		<StructureSection load='4dmo' size='340' side='right' caption='[[4dmo]], [[Resolution\|resolution]] 2.14Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4dmo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bacillus_cereus_atcc_14579 Bacillus cereus atcc 14579~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DMO FirstGlance]. <br>		<table><tr><td colspan='2'>[[4dmo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baccr Baccr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DMO FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KH2:3-(1-METHYLPIPERIDINIUM-1-YL)PROPANE-1-SULFONATE'>KH2</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KH2:3-(1-METHYLPIPERIDINIUM-1-YL)PROPANE-1-SULFONATE'>KH2</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BC_3483, NAT3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=226900 ~~Bacillus cereus ATCC 14579~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BC_3483, NAT3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=226900 BACCR])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-hydroxyarylamine_O-acetyltransferase N-hydroxyarylamine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.118 2.3.1.118] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-hydroxyarylamine_O-acetyltransferase N-hydroxyarylamine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.118 2.3.1.118] </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=4dmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dmo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dmo RCSB], [http://www.ebi.ac.uk/pdbsum/4dmo 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=4dmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dmo OCA], [http://pdbe.org/4dmo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dmo RCSB], [http://www.ebi.ac.uk/pdbsum/4dmo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dmo ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 16:		Line 17:
	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 4dmo" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Bacillus cereus atcc 14579~~]]		[[Category: Baccr]]
	[[Category: N-hydroxyarylamine O-acetyltransferase]]		[[Category: N-hydroxyarylamine O-acetyltransferase]]
	[[Category: Haouz, A]]		[[Category: Haouz, A]]

OCA at 08:55, 21 December 2014

2014-12-21T08:55:15Z

← Older revision		Revision as of 08:55, 21 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_4dmo\| PDB=4dmo \| SCENE= }}~~		==Crystal structure of the (BACCR)NAT3 arylamine N-acetyltransferase from Bacillus cereus reveals a unique Cys-His-Glu catalytic triad==
	===Crystal structure of the (BACCR)NAT3 arylamine N-acetyltransferase from Bacillus cereus reveals a unique Cys-His-Glu catalytic triad===		<StructureSection load='4dmo' size='340' side='right' caption='[[4dmo]], [[Resolution\|resolution]] 2.14Å' scene=''>
	~~{{ABSTRACT_PUBMED_23770703}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4dmo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus_atcc_14579 Bacillus cereus atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DMO FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KH2:3-(1-METHYLPIPERIDINIUM-1-YL)PROPANE-1-SULFONATE'>KH2</scene></td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BC_3483, NAT3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=226900 Bacillus cereus ATCC 14579])</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-hydroxyarylamine_O-acetyltransferase N-hydroxyarylamine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.118 2.3.1.118] </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=4dmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dmo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dmo RCSB], [http://www.ebi.ac.uk/pdbsum/4dmo PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Arylamine N-acetyltransferases (NAT), a class of xenobiotic-metabolizing enzymes, catalyze the acetylation of aromatic amine compounds through a strictly conserved Cys-His-Asp catalytic triad. Each residue is essential for catalysis in both prokaryotic and eukaryotic NATs. Indeed, in (HUMAN)NAT2 variants, mutation of the Asp residue to Asn, Gln, or Glu dramatically impairs enzyme activity. However, a putative atypical NAT harboring a catalytic triad Glu residue was recently identified in Bacillus cereus [(BACCR)NAT3], but has not yet been characterized. We report here the crystal structure and functional characterization of this atypical NAT. The overall fold of (BACCR)NAT3 and the geometry of its Cys-His-Glu catalytic triad are similar to those present in functional NATs. Importantly, the enzyme was found to be active and to acetylate prototypic arylamine NAT substrates. In contrast to human NAT2, the presence of a Glu or Asp in the triad of (BACCR)NAT3 did not significantly affect enzyme structure or function. Computational analysis identified differences in residue packing and steric constraints in the active site of (BACCR)NAT3 that allow it to accommodate a Cys-His-Glu triad. These findings overturn the conventional view, demonstrating that the catalytic triad of this family of acetyltransferases is plastic. Moreover, they highlight the need for further study of the evolutionary history of NATs and the functional significance of the predominant Cys-His-Asp triad in both prokaryotic and eukaryotic forms.

	~~==About this Structure==~~		Structural and biochemical characterization of an active arylamine N-acetyltransferase possessing a non-canonical Cys-His-Glu catalytic triad.,Kubiak X, de la Sierra-Gallay IL, Chaffotte AF, Pluvinage B, Weber P, Haouz A, Dupret JM, Rodrigues-Lima F J Biol Chem. 2013 Jun 19. PMID:23770703<ref>PMID:23770703</ref>
	~~[[4dmo]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Bacillus_cereus_atcc_14579 Bacillus cereus atcc 14579]~~. ~~Full crystallographic information is available from [http~~:/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4DMO OCA].~~

	==~~Reference~~==		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~<ref group="xtra">PMID:023770703</ref>~~<references ~~group="xtra"~~/><~~references~~/>		</div>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
	[[Category: Bacillus cereus atcc 14579]]		[[Category: Bacillus cereus atcc 14579]]
	[[Category: N-hydroxyarylamine O-acetyltransferase]]		[[Category: N-hydroxyarylamine O-acetyltransferase]]
	[[Category: Haouz, A.]]		[[Category: Haouz, A]]
	[[Category: Kubiak, X.]]		[[Category: Kubiak, X]]
	[[Category: Rodrigues-Lima, F.]]		[[Category: Rodrigues-Lima, F]]
	[[Category: Sierra-Gallay, I Li de la.]]		[[Category: Sierra-Gallay, I Li de la]]
	[[Category: Weber, P.]]		[[Category: Weber, P]]
	[[Category: Acetyltransferase]]		[[Category: Acetyltransferase]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 14:05, 3 July 2013

2013-07-03T14:05:09Z

← Older revision		Revision as of 14:05, 3 July 2013
Line 4:		Line 4:

	==About this Structure==		==About this Structure==
	[[4dmo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DMO OCA].		[[4dmo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus_atcc_14579 Bacillus cereus atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DMO OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:023770703</ref><references group="xtra"/><references/>		<ref group="xtra">PMID:023770703</ref><references group="xtra"/><references/>
			[[Category: Bacillus cereus atcc 14579]]
	[[Category: N-hydroxyarylamine O-acetyltransferase]]		[[Category: N-hydroxyarylamine O-acetyltransferase]]
	[[Category: Haouz, A.]]		[[Category: Haouz, A.]]

OCA at 10:49, 3 July 2013

2013-07-03T10:49:01Z

← Older revision		Revision as of 10:49, 3 July 2013
Line 1:		Line 1:
	{{STRUCTURE_4dmo\| PDB=4dmo \| SCENE= }}		{{STRUCTURE_4dmo\| PDB=4dmo \| SCENE= }}
	===Crystal structure of the (BACCR)NAT3 arylamine N-acetyltransferase from Bacillus cereus reveals a unique Cys-His-Glu catalytic triad===		===Crystal structure of the (BACCR)NAT3 arylamine N-acetyltransferase from Bacillus cereus reveals a unique Cys-His-Glu catalytic triad===
			{{ABSTRACT_PUBMED_23770703}}

	==About this Structure==		==About this Structure==
	[[4dmo]] is a 2 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus_atcc_14579 Bacillus cereus atcc 14579]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DMO OCA].		[[4dmo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DMO OCA].
	~~[[Category~~: ~~Bacillus cereus atcc 14579]]~~
			==Reference==
			<ref group="xtra">PMID:023770703</ref><references group="xtra"/><references/>
	[[Category: N-hydroxyarylamine O-acetyltransferase]]		[[Category: N-hydroxyarylamine O-acetyltransferase]]
	[[Category: Haouz, A.]]		[[Category: Haouz, A.]]

OCA at 10:23, 30 June 2013

2013-06-30T10:23:25Z

← Older revision		Revision as of 10:23, 30 June 2013
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	~~'''Unreleased~~ structure~~'''~~		{{STRUCTURE_4dmo\| PDB=4dmo \| SCENE= }}
			===Crystal structure of the (BACCR)NAT3 arylamine N-acetyltransferase from Bacillus cereus reveals a unique Cys-His-Glu catalytic triad===

	~~The entry~~ 4dmo is ~~ON HOLD until Aug 07 2014~~		==About this Structure==
			[[4dmo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus_atcc_14579 Bacillus cereus atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DMO OCA].
	~~Authors~~: Kubiak, X., ~~Li de la~~ Sierra-Gallay, I.~~, Haouz, A.,~~ Weber, P.~~, Rodrigues-Lima, F.~~		[[Category: Bacillus cereus atcc 14579]]
			[[Category: N-hydroxyarylamine O-acetyltransferase]]
	~~Description~~: ~~Crystal structure of the (BACCR)NAT3 arylamine N-acetyltransferase from Bacillus cereus reveals a unique Cys-His-Glu catalytic triad~~		[[Category: Haouz, A.]]
			[[Category: Kubiak, X.]]
			[[Category: Rodrigues-Lima, F.]]
			[[Category: Sierra-Gallay, I Li de la.]]
			[[Category: Weber, P.]]
			[[Category: Acetyltransferase]]
			[[Category: Transferase]]

OCA at 10:59, 19 June 2013

2013-06-19T10:59:21Z

← Older revision		Revision as of 10:59, 19 June 2013
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4dmo is ON HOLD		The entry 4dmo is ON HOLD until Aug 07 2014

	Authors: Kubiak, X., Li de la Sierra-Gallay, I., Haouz, A., Weber, P., Rodrigues-Lima, F.		Authors: Kubiak, X., Li de la Sierra-Gallay, I., Haouz, A., Weber, P., Rodrigues-Lima, F.

	Description: Crystal structure of the (BACCR)NAT3 arylamine N-acetyltransferase from Bacillus cereus reveals a unique Cys-His-Glu catalytic triad		Description: Crystal structure of the (BACCR)NAT3 arylamine N-acetyltransferase from Bacillus cereus reveals a unique Cys-His-Glu catalytic triad

OCA at 06:57, 2 May 2013

2013-05-02T06:57:49Z

← Older revision		Revision as of 06:57, 2 May 2013
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4dmo is ON HOLD ~~until May 07 2014~~		The entry 4dmo is ON HOLD

	Authors: Kubiak, X., Li de la Sierra-Gallay, I., Haouz, A., Weber, P., Rodrigues-Lima, F.		Authors: Kubiak, X., Li de la Sierra-Gallay, I., Haouz, A., Weber, P., Rodrigues-Lima, F.

	Description: Crystal structure of the (BACCR)NAT3 arylamine N-acetyltransferase from Bacillus cereus reveals a unique Cys-His-Glu catalytic triad		Description: Crystal structure of the (BACCR)NAT3 arylamine N-acetyltransferase from Bacillus cereus reveals a unique Cys-His-Glu catalytic triad