OCA at 14:39, 20 September 2023

OCA — Wed, 20 Sep 2023 14:39:30 GMT

←Older revision		Revision as of 14:39, 20 September 2023
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-	'''Unreleased structure'''

-	~~The entry~~ 8bre is ~~ON HOLD until Paper~~ Publication	+	==1,6-anhydro-n-actetylmuramic acid kinase (AnmK)==
		+	<StructureSection load='8bre' size='340' side='right'caption='[[8bre]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8bre]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BRE FirstGlance]. <br>
		+	</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=CL:CHLORIDE+ION'>CL</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=8bre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bre OCA], [https://pdbe.org/8bre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bre RCSB], [https://www.ebi.ac.uk/pdbsum/8bre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bre ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/ANMK_PSEAE ANMK_PSEAE] Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The bacterial cell envelope is the structure with which the bacterium both engages with, and is protected from, its environment. Within this envelop is a conserved peptidoglycan polymer which confers shape and strength to the cell envelop. The enzymatic processes that build, remodel, and recycle the chemical components of this cross-linked polymer are preeminent targets of antibiotics, and exploratory targets for emerging antibiotic structures. We report a comprehensive kinetic and structural analysis for one such enzyme, the Pseudomonas aeruginosa anhydro-N-acetylmuramic acid (anhNAM) kinase (AnmK). AnmK is an important enzyme in the peptidoglycan-recycling pathway of this pathogen. It catalyzes the remarkable pairing of hydrolytic ring-opening of anhNAM with concomitant ATP-dependent phosphoryl transfer. AnmK follows a random-sequential kinetic mechanism with respect to its anhNAM and ATP substrates. Crystallographic analyses of four distinct structures (apo AnmK, AnmK:AMPPNP, AnmK:AMPPNP:anhNAM and AnmK:ATP:anhNAM) demonstrate that both substrates enter the active site independently in an ungated conformation of the substrate subsites, with protein loops acting as gates for anhNAM binding. Catalysis occurs within a closed conformational state for the enzyme. We observe this state crystallographically using ATP-mimetic molecules. A remarkable X-ray structure for dimeric AnmK sheds light on the pre-catalytic and post-catalytic ternary complexes, one in each subunit. Computational simulations in conjunction with the four high-resolution X-ray structures reveal the full catalytic cycle. We further report that a P. aeruginosa strain with disrupted anmK gene is more susceptible to the beta-lactam imipenem compared to the wild-type strain. These observations position AnmK for understanding the nexus among peptidoglycan recycling, susceptibility to antibiotics, and bacterial virulence.

-	~~Authors~~:	+	Catalytic process of anhydro-N-acetylmuramic acid kinase (AnmK) from Pseudomonas aeruginosa.,El-Araby AM, Jimenez-Faraco E, Feltzer R, Martin-Garcia JM, Karri BR, Ramachandran B, Kim C, Fisher JF, Hermoso JA, Mobashery S J Biol Chem. 2023 Sep 1:105198. doi: 10.1016/j.jbc.2023.105198. PMID:37660917<ref>PMID:37660917</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 8bre" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Pseudomonas aeruginosa]]
		+	[[Category: Hermoso JA]]
		+	[[Category: Jimenez-Faraco E]]

OCA at 18:33, 12 April 2023

OCA — Wed, 12 Apr 2023 18:33:39 GMT

←Older revision		Revision as of 18:33, 12 April 2023
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8bre is ON HOLD	+	The entry 8bre is ON HOLD until Paper Publication

	Authors:		Authors:

OCA at 05:26, 8 March 2023

OCA — Wed, 08 Mar 2023 05:26:23 GMT

←Older revision		Revision as of 05:26, 8 March 2023
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8bre is ON HOLD ~~until Paper Publication~~	+	The entry 8bre is ON HOLD

	Authors:		Authors:

OCA at 05:27, 28 December 2022

OCA — Wed, 28 Dec 2022 05:27:57 GMT

←Older revision		Revision as of 05:27, 28 December 2022
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8bre is ON HOLD	+	The entry 8bre is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "8bre" [edit=sysop:move=sysop]

OCA — Wed, 30 Nov 2022 08:27:37 GMT

Protected "8bre" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:27, 30 November 2022

OCA: New page: '''Unreleased structure''' The entry 8bre is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 30 Nov 2022 08:27:36 GMT

New page: '''Unreleased structure''' The entry 8bre is ON HOLD Authors: Description: Category: Unreleased Structures

New page