4e1k - Revision history

OCA at 11:01, 1 March 2024

2024-03-01T11:01:15Z

← Older revision		Revision as of 11:01, 1 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e1k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae_Rd_KW20 Haemophilus influenzae Rd KW20]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E1K FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e1k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae_Rd_KW20 Haemophilus influenzae Rd KW20]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E1K FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0N5:N-{4-[(7-HYDROXY-6-METHOXYQUINAZOLIN-4-YL)AMINO]PHENYL}BENZAMIDE'>0N5</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0N5:N-{4-[(7-HYDROXY-6-METHOXYQUINAZOLIN-4-YL)AMINO]PHENYL}BENZAMIDE'>0N5</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4e1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1k OCA], [https://pdbe.org/4e1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e1k RCSB], [https://www.ebi.ac.uk/pdbsum/4e1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e1k 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=4e1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1k OCA], [https://pdbe.org/4e1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e1k RCSB], [https://www.ebi.ac.uk/pdbsum/4e1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e1k ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/GLMU_HAEIN GLMU_HAEIN]] Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.<ref>PMID:18029420</ref>		[https://www.uniprot.org/uniprot/GLMU_HAEIN GLMU_HAEIN] Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.<ref>PMID:18029420</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	GlmU is a bifunctional enzyme with acetyltransferase and uridyltransferase activities, and is essential for the biosynthesis of the bacterial cell wall. Inhibition results in a loss of cell viability. GlmU is therefore considered a potential target for novel antibacterial agents. A HTS (high-throughput screen) identified a series of aminoquinazolines with submicromolar potency against the uridyltransferase reaction. Biochemical and biophysical characterization showed competition with UTP binding. We determined the crystal structure of a representative aminoquinazoline bound to the Haemophilus influenzae isoenzyme at a resolution of 2.0 A. The inhibitor occupies part of the UTP site, skirts the outer perimeter of the GlcNAc1-P (N-acetylglucosamine-1-phosphate) pocket and anchors a hydrophobic moiety into a lipophilic pocket. Our SAR (structure-activity relationship) analysis shows that all of these interactions are essential for inhibitory activity in this series. The crystal structure suggests that the compound would block binding of UTP and lock GlmU in an apo-enzyme-like conformation, thus interfering with its enzymatic activity. Our lead generation effort provides ample scope for further optimization of these compounds for antibacterial drug discovery.

	An aminoquinazoline inhibitor of the essential bacterial cell wall synthetic enzyme GlmU has a unique non-protein-kinase-like binding mode.,Larsen NA, Nash TJ, Morningstar M, Shapiro AB, Joubran C, Blackett CJ, Patten AD, Boriack-Sjodin PA, Doig P Biochem J. 2012 Sep 15;446(3):405-13. doi: 10.1042/BJ20120596. PMID:22721802<ref>PMID:22721802</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4e1k" style="background-color:#fffaf0;"></div~~>

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

OCA at 06:45, 28 September 2022

2022-09-28T06:45:02Z

← Older revision		Revision as of 06:45, 28 September 2022
Line 1:		Line 1:

	==GlmU in complex with a Quinazoline Compound==		==GlmU in complex with a Quinazoline Compound==
	<StructureSection load='4e1k' size='340' side='right' caption='[[4e1k]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4e1k' size='340' side='right'caption='[[4e1k]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e1k]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Haein Haein~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1K OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4E1K FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e1k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae_Rd_KW20 Haemophilus influenzae Rd KW20]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E1K FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0N5:N-{4-[(7-HYDROXY-6-METHOXYQUINAZOLIN-4-YL)AMINO]PHENYL}BENZAMIDE'>0N5</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~</td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0N5:N-{4-[(7-HYDROXY-6-METHOXYQUINAZOLIN-4-YL)AMINO]PHENYL}BENZAMIDE'>0N5</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">glmU, HI_0642 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=71421 HAEIN])~~</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=4e1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1k OCA], [https://pdbe.org/4e1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e1k RCSB], [https://www.ebi.ac.uk/pdbsum/4e1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e1k 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=4e1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1k OCA], [~~http~~://pdbe.org/4e1k PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4e1k RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4e1k PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4e1k ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/GLMU_HAEIN GLMU_HAEIN]] Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.<ref>PMID:18029420</ref>		[[https://www.uniprot.org/uniprot/GLMU_HAEIN GLMU_HAEIN]] Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.<ref>PMID:18029420</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 19:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4e1k" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4e1k" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[N-acetylglucosamine-1-phosphate uridyltransferase\|N-acetylglucosamine-1-phosphate uridyltransferase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Haein~~]]		[[Category: Haemophilus influenzae Rd KW20]]
	[[Category: ~~Doig, P~~]]		[[Category: Large Structures]]
	[[Category: ~~Larsen, N A~~]]		[[Category: Doig P]]
	[[Category: ~~Acyltransferase]]~~		[[Category: Larsen NA]]
	~~[[Category: Cell shape]]~~
	~~[[Category: Cell wall biogenesis/degradation]]~~
	~~[[Category: Metal-binding]]~~
	~~[[Category: Multifunctional enzyme]]~~
	~~[[Category: Nucleotidyl transferase]]~~
	~~[[Category: Peptidoglycan synthesis]]~~
	~~[[Category: Transferase-transferase inhibitor complex]]~~
	~~[[Category: Uridyltransferase~~]]

OCA at 12:41, 5 August 2016

2016-08-05T12:41:57Z

← Older revision		Revision as of 12:41, 5 August 2016
Line 1:		Line 1:

	==GlmU in complex with a Quinazoline Compound==		==GlmU in complex with a Quinazoline Compound==
	<StructureSection load='4e1k' size='340' side='right' caption='[[4e1k]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4e1k' size='340' side='right' caption='[[4e1k]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e1k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Haemophilus_influenzae_rd_kw20 Haemophilus influenzae rd kw20~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E1K FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e1k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Haein Haein]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E1K FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0N5:N-{4-[(7-HYDROXY-6-METHOXYQUINAZOLIN-4-YL)AMINO]PHENYL}BENZAMIDE'>0N5</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0N5:N-{4-[(7-HYDROXY-6-METHOXYQUINAZOLIN-4-YL)AMINO]PHENYL}BENZAMIDE'>0N5</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">glmU, HI_0642 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=71421 ~~Haemophilus influenzae Rd KW20~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">glmU, HI_0642 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=71421 HAEIN])</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=4e1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e1k RCSB], [http://www.ebi.ac.uk/pdbsum/4e1k 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=4e1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1k OCA], [http://pdbe.org/4e1k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e1k RCSB], [http://www.ebi.ac.uk/pdbsum/4e1k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e1k 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 4e1k" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Haemophilus influenzae rd kw20~~]]		[[Category: Haein]]
	[[Category: Doig, P]]		[[Category: Doig, P]]
	[[Category: Larsen, N A]]		[[Category: Larsen, N A]]

OCA at 02:32, 25 December 2014

2014-12-25T02:32:59Z

← Older revision		Revision as of 02:32, 25 December 2014
Line 7:		Line 7:
	<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=4e1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e1k RCSB], [http://www.ebi.ac.uk/pdbsum/4e1k 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=4e1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e1k RCSB], [http://www.ebi.ac.uk/pdbsum/4e1k PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/GLMU_HAEIN GLMU_HAEIN]] Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.<ref>PMID:18029420</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 11:40, 21 December 2014

2014-12-21T11:40:58Z

← Older revision		Revision as of 11:40, 21 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_4e1k\| PDB~~=4e1k \| ~~SCENE~~= }}		==GlmU in complex with a Quinazoline Compound==
	===~~GlmU in complex~~ with a ~~Quinazoline Compound~~===		<StructureSection load='4e1k' size='340' side='right' caption='[[4e1k]], [[Resolution\|resolution]] 2.00Å' scene=''>
	{{~~ABSTRACT_PUBMED_22721802}~~}		== Structural highlights ==
			<table><tr><td colspan='2'>[[4e1k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae_rd_kw20 Haemophilus influenzae rd kw20]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E1K FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0N5:N-{4-[(7-HYDROXY-6-METHOXYQUINAZOLIN-4-YL)AMINO]PHENYL}BENZAMIDE'>0N5</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">glmU, HI_0642 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=71421 Haemophilus influenzae Rd KW20])</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=4e1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e1k RCSB], [http://www.ebi.ac.uk/pdbsum/4e1k PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			GlmU is a bifunctional enzyme with acetyltransferase and uridyltransferase activities, and is essential for the biosynthesis of the bacterial cell wall. Inhibition results in a loss of cell viability. GlmU is therefore considered a potential target for novel antibacterial agents. A HTS (high-throughput screen) identified a series of aminoquinazolines with submicromolar potency against the uridyltransferase reaction. Biochemical and biophysical characterization showed competition with UTP binding. We determined the crystal structure of a representative aminoquinazoline bound to the Haemophilus influenzae isoenzyme at a resolution of 2.0 A. The inhibitor occupies part of the UTP site, skirts the outer perimeter of the GlcNAc1-P (N-acetylglucosamine-1-phosphate) pocket and anchors a hydrophobic moiety into a lipophilic pocket. Our SAR (structure-activity relationship) analysis shows that all of these interactions are essential for inhibitory activity in this series. The crystal structure suggests that the compound would block binding of UTP and lock GlmU in an apo-enzyme-like conformation, thus interfering with its enzymatic activity. Our lead generation effort provides ample scope for further optimization of these compounds for antibacterial drug discovery.

	~~==Function==~~		An aminoquinazoline inhibitor of the essential bacterial cell wall synthetic enzyme GlmU has a unique non-protein-kinase-like binding mode.,Larsen NA, Nash TJ, Morningstar M, Shapiro AB, Joubran C, Blackett CJ, Patten AD, Boriack-Sjodin PA, Doig P Biochem J. 2012 Sep 15;446(3):405-13. doi: 10.1042/BJ20120596. PMID:22721802<ref>PMID:22721802</ref>
	~~[[http://www.uniprot.org/uniprot/GLMU_HAEIN GLMU_HAEIN]] Catalyzes~~ the ~~last two sequential reactions in the de novo biosynthetic pathway for UDP~~-N-~~acetylglucosamine (UDP~~-~~GlcNAc)~~. ~~The~~ C-~~terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-~~P~~) to produce N-acetylglucosamine-1-phosphate~~ (~~GlcNAc-1-P~~)~~, which is converted into UDP~~-~~GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain~~.<ref>PMID:~~18029420~~</ref>

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[4e1k]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Haemophilus_influenzae_rd_kw20 Haemophilus influenzae rd kw20]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4E1K OCA].~~		</div>
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:022721802</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
	[[Category: Haemophilus influenzae rd kw20]]		[[Category: Haemophilus influenzae rd kw20]]
	[[Category: Doig, P.]]		[[Category: Doig, P]]
	[[Category: Larsen, N A.]]		[[Category: Larsen, N A]]
	[[Category: Acyltransferase]]		[[Category: Acyltransferase]]
	[[Category: Cell shape]]		[[Category: Cell shape]]

OCA at 16:03, 19 June 2013

2013-06-19T16:03:57Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+{{STRUCTURE_4e1k|  PDB=4e1k  |  SCENE=  }}
-The entry 4e1k is ON HOLD  until Paper Publication
+==Function==
-Authors: Larsen, N.A., Doig, P.
+==About this Structure==
-Description: GlmU in complex with a Quinazoline Compound
+==Reference==

OCA at 19:43, 17 April 2013

2013-04-17T19:43:44Z

← Older revision		Revision as of 19:43, 17 April 2013
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4e1k is ON HOLD		The entry 4e1k is ON HOLD until Paper Publication

	Authors: Larsen, N.A., Doig, P.		Authors: Larsen, N.A., Doig, P.

	Description: GlmU in complex with a Quinazoline Compound		Description: GlmU in complex with a Quinazoline Compound

OCA at 07:14, 21 March 2012

2012-03-21T07:14:36Z

← Older revision		Revision as of 07:14, 21 March 2012
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	Authors: Larsen, N.A., Doig, P.		Authors: Larsen, N.A., Doig, P.

	Description: GlmU in complex with ~~AstraZeneca~~ Quinazoline Compound		Description: GlmU in complex with a Quinazoline Compound

OCA: Protected "4e1k" [edit=sysop:move=sysop]

2012-03-14T06:16:06Z

Protected "4e1k" [edit=sysop:move=sysop]

← Older revision	Revision as of 06:16, 14 March 2012
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4e1k is ON HOLD Authors: Larsen, N.A., Doig, P. Description: GlmU in complex with AstraZeneca Quinazoline Compound

2012-03-14T06:16:05Z

New page: '''Unreleased structure''' The entry 4e1k is ON HOLD Authors: Larsen, N.A., Doig, P. Description: GlmU in complex with AstraZeneca Quinazoline Compound

New page

'''Unreleased structure'''

The entry 4e1k is ON HOLD

Authors: Larsen, N.A., Doig, P.

Description: GlmU in complex with AstraZeneca Quinazoline Compound