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| | <StructureSection load='4bxj' size='340' side='right'caption='[[4bxj]], [[Resolution|resolution]] 2.35Å' scene=''> | | <StructureSection load='4bxj' size='340' side='right'caption='[[4bxj]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4bxj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BXJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BXJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4bxj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BXJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BXJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.35Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bxd|4bxd]], [[4bxe|4bxe]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylmuramoyl-L-alanine_amidase N-acetylmuramoyl-L-alanine amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.28 3.5.1.28] </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=4bxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bxj OCA], [https://pdbe.org/4bxj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bxj RCSB], [https://www.ebi.ac.uk/pdbsum/4bxj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bxj 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=4bxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bxj OCA], [http://pdbe.org/4bxj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bxj RCSB], [http://www.ebi.ac.uk/pdbsum/4bxj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bxj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9I5D1_PSEAE Q9I5D1_PSEAE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: N-acetylmuramoyl-L-alanine amidase]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Pseae]]
| + | [[Category: Carrasco-Lopez C]] |
| - | [[Category: Carrasco-Lopez, C]] | + | [[Category: Hermoso JA]] |
| - | [[Category: Hermoso, J A]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
Q9I5D1_PSEAE
Publication Abstract from PubMed
Bacterial cell wall is a polymer of considerable complexity that is in constant equilibrium between synthesis and recycling. AmpDh3 is a periplasmic zinc protease of Pseudomonas aeruginosa , which is intimately involved in cell-wall remodeling. We document the hydrolytic reactions that this enzyme performs on the cell wall. The process removes the peptide stems from the peptidoglycan, the major constituent of the cell wall. We document that the majority of the reactions of this enzyme takes place on the polymeric insoluble portion of the cell wall, as opposed to the fraction that is released from it. We show that AmpDh3 is tetrameric both in crystals and in solution. Based on the X-ray structures of the enzyme in complex with two synthetic cell-wall-based ligands, we present for the first time a model for a multivalent anchoring of AmpDh3 onto the cell wall, which lends itself to its processive remodeling.
Cell-Wall Remodeling by the Zinc-Protease AmpDh3 from Pseudomonas aeruginosa.,Lee M, Artola-Recolons C, Carrasco-Lopez C, Martinez-Caballero S, Hesek D, Spink E, Lastochkin E, Zhang W, Hellman LM, Boggess B, Hermoso JA, Mobashery S J Am Chem Soc. 2013 Aug 28;135(34):12604-7. doi: 10.1021/ja407445x. Epub 2013 Aug, 15. PMID:23931161[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lee M, Artola-Recolons C, Carrasco-Lopez C, Martinez-Caballero S, Hesek D, Spink E, Lastochkin E, Zhang W, Hellman LM, Boggess B, Hermoso JA, Mobashery S. Cell-Wall Remodeling by the Zinc-Protease AmpDh3 from Pseudomonas aeruginosa. J Am Chem Soc. 2013 Aug 28;135(34):12604-7. doi: 10.1021/ja407445x. Epub 2013 Aug, 15. PMID:23931161 doi:http://dx.doi.org/10.1021/ja407445x
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