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4mo5

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==Crystal structure of AnmK bound to AMPPCP and anhMurNAc==
==Crystal structure of AnmK bound to AMPPCP and anhMurNAc==
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<StructureSection load='4mo5' size='340' side='right' caption='[[4mo5]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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<StructureSection load='4mo5' size='340' side='right'caption='[[4mo5]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4mo5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MO5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MO5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4mo5]] is a 4 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=4MO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MO5 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=AH0:2-(2-ACETYLAMINO-4-HYDROXY-6,8-DIOXA-BICYCLO[3.2.1]OCT-3-YLOXY)-PROPIONIC+ACID'>AH0</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mo4|4mo4]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=AH0:2-(2-ACETYLAMINO-4-HYDROXY-6,8-DIOXA-BICYCLO[3.2.1]OCT-3-YLOXY)-PROPIONIC+ACID'>AH0</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">anmK, PA0666 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4mo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mo5 OCA], [https://pdbe.org/4mo5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mo5 RCSB], [https://www.ebi.ac.uk/pdbsum/4mo5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mo5 ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Anhydro-N-acetylmuramic_acid_kinase Anhydro-N-acetylmuramic acid kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.170 2.7.1.170] </span></td></tr>
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<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=4mo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mo5 OCA], [http://pdbe.org/4mo5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mo5 RCSB], [http://www.ebi.ac.uk/pdbsum/4mo5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mo5 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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).
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[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Anhydro-sugar kinases are unique from other sugar kinases in that they must cleave the 1,6-anhydro ring of their sugar substrate in order to phosphorylate it using ATP. Here we show that the peptidoglycan recycling enzyme 1,6-Anhydro-N-acetylmuramic acid kinase (AnmK) from Pseudomonas aeruginosa undergoes large conformational changes during its catalytic cycle, with its two domains rotating apart by up to 32 degrees around two hinge regions to expose an active site cleft into which the substrates 1,6-anhydroMurNAc and ATP can bind. X-ray structures of the open state bound to a nonhydrolyzable ATP analogue (AMPPCP) and 1,6-anhydroMurNAc provides detailed insight into a ternary complex that forms preceding an operative Michaelis complex. Structural analysis of the hinge regions demonstrates a role for nucleotide binding and possible cross-talk between the bound ligands to modulate the opening and closing of AnmK. Though AnmK was found to exhibit similar binding affinities for ATP, ADP and AMPPCP according to fluorescence spectroscopy, SAXS analyses revealed that AnmK adopts an open conformation in solution in the absence of ligand, and that it remains in this open state after binding AMPPCP, as we had observed for our crystal structure of this complex. In contrast, the enzyme favoured a closed conformation when bound to ADP in solution, consistent with a previous crystal structure of this complex. Together, our findings show that the open conformation of AnmK facilitates binding of both the sugar and nucleotide substrates, and that large structural rearrangements must occur upon closure of the enzyme to correctly align the substrates and residues of the enzyme for catalysis.
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Conformational itinerary of Pseudomonas aeruginosa 1,6-Anhydro-N-acetylmuramic acid kinase during its catalytic cycle.,Bacik JP, Tavassoli M, Patel TR, McKenna SA, Vocadlo DJ, Khajehpour M, Mark BL J Biol Chem. 2013 Dec 20. PMID:24362022<ref>PMID:24362022</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4mo5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Anhydro-N-acetylmuramic acid kinase]]
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[[Category: Large Structures]]
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[[Category: Bacik, J P]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Mark, B L]]
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[[Category: Bacik JP]]
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[[Category: Atp binding]]
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[[Category: Mark BL]]
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[[Category: Atpase domain]]
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[[Category: Kinase]]
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[[Category: Transferase]]
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Current revision

Crystal structure of AnmK bound to AMPPCP and anhMurNAc

PDB ID 4mo5

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