4ri1 - Revision history

OCA at 12:52, 1 March 2024

OCA — Fri, 01 Mar 2024 12:52:42 GMT

←Older revision		Revision as of 12:52, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ri1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RI1 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ri1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RI1 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</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]] 2.3Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=4ri1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ri1 OCA], [https://pdbe.org/4ri1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ri1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ri1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ri1 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=4ri1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ri1 OCA], [https://pdbe.org/4ri1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ri1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ri1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ri1 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/PSEH_HELPY PSEH_HELPY] Catalyzes the third step in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. Mediates N-4 acetylation of UDP-4-amino-4,6-dideoxy-beta-L-AltNAc to form UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose.<ref>PMID:16751642</ref>		[https://www.uniprot.org/uniprot/PSEH_HELPY PSEH_HELPY] Catalyzes the third step in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. Mediates N-4 acetylation of UDP-4-amino-4,6-dideoxy-beta-L-AltNAc to form UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose.<ref>PMID:16751642</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Helicobacter pylori infection is the common cause of gastroduodenal diseases linked to a higher risk of the development of gastric cancer. Persistent infection requires functional flagella that are heavily glycosylated with 5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-L-manno-nonulosonic acid (pseudaminic acid). Pseudaminic acid biosynthesis protein H (PseH) catalyzes the third step in its biosynthetic pathway, producing UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose. It belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The crystal structure of the PseH complex with cofactor acetyl-CoA has been determined at 2.3 A resolution. This is the first crystal structure of the GNAT superfamily member with specificity to UDP-4-amino-4,6-dideoxy-beta-L-AltNAc. PseH is a homodimer in the crystal, each subunit of which has a central twisted beta-sheet flanked by five alpha-helices and is structurally homologous to those of other GNAT superfamily enzymes. Interestingly, PseH is more similar to the GNAT enzymes that utilize amino acid sulfamoyl adenosine or protein as a substrate than a different GNAT-superfamily bacterial nucleotide-sugar N-acetyltransferase of the known structure, WecD. Analysis of the complex of PseH with acetyl-CoA revealed the location of the cofactor-binding site between the splayed strands beta4 and beta5. The structure of PseH, together with the conservation of the active-site general acid among GNAT superfamily transferases, are consistent with a common catalytic mechanism for this enzyme that involves direct acetyl transfer from AcCoA without an acetylated enzyme intermediate. Based on structural homology with microcin C7 acetyltransferase MccE and WecD, the Michaelis complex can be modeled. The model suggests that the nucleotide- and 4-amino-4,6-dideoxy-beta-L-AltNAc-binding pockets form extensive interactions with the substrate and are thus the most significant determinants of substrate specificity. A hydrophobic pocket accommodating the 6'-methyl group of the altrose dictates preference to the methyl over the hydroxyl group and thus to contributes to substrate specificity of PseH.
-
-	Crystal Structure of Helicobacter pylori Pseudaminic Acid Biosynthesis N-Acetyltransferase PseH: Implications for Substrate Specificity and Catalysis.,Ud-Din AI, Liu YC, Roujeinikova A PLoS One. 2015 Mar 17;10(3):e0115634. doi: 10.1371/journal.pone.0115634., eCollection 2015. PMID:25781966<ref>PMID:25781966</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4ri1" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:57, 2 March 2023

OCA — Thu, 02 Mar 2023 06:57:37 GMT

←Older revision		Revision as of 06:57, 2 March 2023
Line 3:		Line 3:
	<StructureSection load='4ri1' size='340' side='right'caption='[[4ri1]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='4ri1' size='340' side='right'caption='[[4ri1]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ri1]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Campylobacter_pylori Campylobacter~~ pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RI1 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4RI1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ri1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RI1 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HP0327, HP_0327, pseH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Campylobacter pylori])</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=4ri1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ri1 OCA], [https://pdbe.org/4ri1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ri1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ri1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ri1 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/UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine_N-acetyltransferase UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.202 2.3.1.202] </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=4ri1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ri1 OCA], [~~http~~://pdbe.org/4ri1 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ri1 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ri1 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ri1 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PSEH_HELPY PSEH_HELPY]] Catalyzes the third step in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. Mediates N-4 acetylation of UDP-4-amino-4,6-dideoxy-beta-L-AltNAc to form UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose.<ref>PMID:16751642</ref>	+	[https://www.uniprot.org/uniprot/PSEH_HELPY PSEH_HELPY] Catalyzes the third step in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. Mediates N-4 acetylation of UDP-4-amino-4,6-dideoxy-beta-L-AltNAc to form UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose.<ref>PMID:16751642</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Campylobacter~~ pylori]]	+	[[Category: Helicobacter pylori 26695]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase]]~~	+	[[Category: Roujeinikova A]]
-	[[Category: Roujeinikova, A]]	+	[[Category: Ud-Din AI]]
-	[[Category: Ud-Din~~, A I]]~~	+
-	~~[[Category: Acetyl-coa]]~~	+
-	~~[[Category: Gnat family]]~~	+
-	~~[[Category: N-acetyl transferase]]~~	+
-	~~[[Category: None]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 10:31, 1 May 2019

OCA — Wed, 01 May 2019 10:31:29 GMT

←Older revision		Revision as of 10:31, 1 May 2019
Line 1:		Line 1:

	==Crystal structure of Helicobacter pylori pseudaminic acid biosynthesis N -acetyltransferase PseH complex with acetyl-coA==		==Crystal structure of Helicobacter pylori pseudaminic acid biosynthesis N -acetyltransferase PseH complex with acetyl-coA==
-	<StructureSection load='4ri1' size='340' side='right' caption='[[4ri1]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='4ri1' size='340' side='right'caption='[[4ri1]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ri1]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RI1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RI1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ri1]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Campylobacter_pylori Campylobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RI1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RI1 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HP0327, HP_0327, pseH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Campylobacter pylori])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine_N-acetyltransferase UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.202 2.3.1.202] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine_N-acetyltransferase UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.202 2.3.1.202] </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=4ri1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ri1 OCA], [http://pdbe.org/4ri1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ri1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ri1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ri1 ProSAT]</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=4ri1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ri1 OCA], [http://pdbe.org/4ri1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ri1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ri1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ri1 ProSAT]</span></td></tr>
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Campylobacter pylori]]
		+	[[Category: Large Structures]]
	[[Category: UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase]]		[[Category: UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase]]
	[[Category: Roujeinikova, A]]		[[Category: Roujeinikova, A]]

OCA at 17:29, 18 January 2017

OCA — Wed, 18 Jan 2017 17:29:54 GMT

←Older revision		Revision as of 17:29, 18 January 2017
Line 1:		Line 1:
		+
	==Crystal structure of Helicobacter pylori pseudaminic acid biosynthesis N -acetyltransferase PseH complex with acetyl-coA==		==Crystal structure of Helicobacter pylori pseudaminic acid biosynthesis N -acetyltransferase PseH complex with acetyl-coA==
	<StructureSection load='4ri1' size='340' side='right' caption='[[4ri1]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='4ri1' size='340' side='right' caption='[[4ri1]], [[Resolution\|resolution]] 2.30Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine_N-acetyltransferase UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.202 2.3.1.202] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine_N-acetyltransferase UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.202 2.3.1.202] </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=4ri1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ri1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ri1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ri1 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=4ri1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ri1 OCA], [http://pdbe.org/4ri1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ri1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ri1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ri1 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4ri1" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:12, 1 April 2015

OCA — Wed, 01 Apr 2015 13:12:07 GMT

←Older revision		Revision as of 13:12, 1 April 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal structure of Helicobacter pylori pseudaminic acid biosynthesis N -acetyltransferase PseH complex with acetyl-coA==
		+	<StructureSection load='4ri1' size='340' side='right' caption='[[4ri1]], [[Resolution\|resolution]] 2.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4ri1]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RI1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RI1 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine_N-acetyltransferase UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.202 2.3.1.202] </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=4ri1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ri1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ri1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ri1 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PSEH_HELPY PSEH_HELPY]] Catalyzes the third step in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. Mediates N-4 acetylation of UDP-4-amino-4,6-dideoxy-beta-L-AltNAc to form UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose.<ref>PMID:16751642</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Helicobacter pylori infection is the common cause of gastroduodenal diseases linked to a higher risk of the development of gastric cancer. Persistent infection requires functional flagella that are heavily glycosylated with 5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-L-manno-nonulosonic acid (pseudaminic acid). Pseudaminic acid biosynthesis protein H (PseH) catalyzes the third step in its biosynthetic pathway, producing UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose. It belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The crystal structure of the PseH complex with cofactor acetyl-CoA has been determined at 2.3 A resolution. This is the first crystal structure of the GNAT superfamily member with specificity to UDP-4-amino-4,6-dideoxy-beta-L-AltNAc. PseH is a homodimer in the crystal, each subunit of which has a central twisted beta-sheet flanked by five alpha-helices and is structurally homologous to those of other GNAT superfamily enzymes. Interestingly, PseH is more similar to the GNAT enzymes that utilize amino acid sulfamoyl adenosine or protein as a substrate than a different GNAT-superfamily bacterial nucleotide-sugar N-acetyltransferase of the known structure, WecD. Analysis of the complex of PseH with acetyl-CoA revealed the location of the cofactor-binding site between the splayed strands beta4 and beta5. The structure of PseH, together with the conservation of the active-site general acid among GNAT superfamily transferases, are consistent with a common catalytic mechanism for this enzyme that involves direct acetyl transfer from AcCoA without an acetylated enzyme intermediate. Based on structural homology with microcin C7 acetyltransferase MccE and WecD, the Michaelis complex can be modeled. The model suggests that the nucleotide- and 4-amino-4,6-dideoxy-beta-L-AltNAc-binding pockets form extensive interactions with the substrate and are thus the most significant determinants of substrate specificity. A hydrophobic pocket accommodating the 6'-methyl group of the altrose dictates preference to the methyl over the hydroxyl group and thus to contributes to substrate specificity of PseH.

-	~~The entry 4ri1 is ON HOLD until Paper Publication~~	+	Crystal Structure of Helicobacter pylori Pseudaminic Acid Biosynthesis N-Acetyltransferase PseH: Implications for Substrate Specificity and Catalysis.,Ud-Din AI, Liu YC, Roujeinikova A PLoS One. 2015 Mar 17;10(3):e0115634. doi: 10.1371/journal.pone.0115634., eCollection 2015. PMID:25781966<ref>PMID:25781966</ref>

-	~~Authors: Roujeinikova~~, A.~~, Ud-Din, A~~.I.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: Crystal structure of Helicobacter pylori pseudaminic acid biosynthesis N -acetyltransferase PseH complex with acetyl-coA~~	+	== References ==
-	~~[[Category: Unreleased Structures]]~~	+	<references/>
-	[[Category: Ud-~~Din~~, ~~A.I~~]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase]]
	[[Category: Roujeinikova, A]]		[[Category: Roujeinikova, A]]
		+	[[Category: Ud-Din, A I]]
		+	[[Category: Acetyl-coa]]
		+	[[Category: Gnat family]]
		+	[[Category: N-acetyl transferase]]
		+	[[Category: None]]
		+	[[Category: Transferase]]

OCA at 16:54, 24 December 2014

OCA — Wed, 24 Dec 2014 16:54:24 GMT

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	Description: Crystal structure of Helicobacter pylori pseudaminic acid biosynthesis N -acetyltransferase PseH complex with acetyl-coA		Description: Crystal structure of Helicobacter pylori pseudaminic acid biosynthesis N -acetyltransferase PseH complex with acetyl-coA
		+	[[Category: Unreleased Structures]]
		+	[[Category: Ud-Din, A.I]]
		+	[[Category: Roujeinikova, A]]

OCA at 09:41, 22 October 2014

OCA — Wed, 22 Oct 2014 09:41:56 GMT

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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4ri1 is ON HOLD	+	The entry 4ri1 is ON HOLD until Paper Publication

	Authors: Roujeinikova, A., Ud-Din, A.I.		Authors: Roujeinikova, A., Ud-Din, A.I.

	Description: Crystal structure of Helicobacter pylori pseudaminic acid biosynthesis N -acetyltransferase PseH complex with acetyl-coA		Description: Crystal structure of Helicobacter pylori pseudaminic acid biosynthesis N -acetyltransferase PseH complex with acetyl-coA

OCA: Protected "4ri1" [edit=sysop:move=sysop]

OCA — Mon, 20 Oct 2014 09:29:12 GMT

Protected "4ri1" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:29, 20 October 2014

OCA: New page: '''Unreleased structure''' The entry 4ri1 is ON HOLD Authors: Roujeinikova, A., Ud-Din, A.I. Description: Crystal structure of Helicobacter pylori pseudaminic acid biosynthesis N -acet...

OCA — Mon, 20 Oct 2014 09:29:10 GMT

New page: '''Unreleased structure''' The entry 4ri1 is ON HOLD Authors: Roujeinikova, A., Ud-Din, A.I. Description: Crystal structure of Helicobacter pylori pseudaminic acid biosynthesis N -acet...

New page

'''Unreleased structure'''

The entry 4ri1 is ON HOLD

Authors: Roujeinikova, A., Ud-Din, A.I.

Description: Crystal structure of Helicobacter pylori pseudaminic acid biosynthesis N -acetyltransferase PseH complex with acetyl-coA