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| | ==Solution structure of Citrobacter Freundii AmpD== | | ==Solution structure of Citrobacter Freundii AmpD== |
| - | <StructureSection load='1j3g' size='340' side='right'caption='[[1j3g]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1j3g' size='340' side='right'caption='[[1j3g]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1j3g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_freundii"_braak_1928 "bacterium freundii" braak 1928]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1iya 1iya] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1j2s 1j2s]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J3G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1j3g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1iya 1iya] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1j2s 1j2s]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J3G FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/N-acetylmuramoyl-L-alanine_amidase N-acetylmuramoyl-L-alanine amidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.28 3.5.1.28] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1j3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j3g OCA], [https://pdbe.org/1j3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j3g RCSB], [https://www.ebi.ac.uk/pdbsum/1j3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j3g 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=1j3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j3g OCA], [https://pdbe.org/1j3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j3g RCSB], [https://www.ebi.ac.uk/pdbsum/1j3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j3g ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/AMPD_CITFR AMPD_CITFR]] Involved in both cell wall peptidoglycans recycling and beta-lactamase induction. Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety.
| + | [https://www.uniprot.org/uniprot/AMPD_CITFR AMPD_CITFR] Involved in both cell wall peptidoglycans recycling and beta-lactamase induction. Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium freundii braak 1928]] | + | [[Category: Citrobacter freundii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: N-acetylmuramoyl-L-alanine amidase]]
| + | [[Category: Dehareng D]] |
| - | [[Category: Dehareng, D]] | + | [[Category: Genereux C]] |
| - | [[Category: Genereux, C]] | + | [[Category: Joris B]] |
| - | [[Category: Joris, B]] | + | [[Category: Liepinsh E]] |
| - | [[Category: Liepinsh, E]] | + | [[Category: Otting G]] |
| - | [[Category: Otting, G]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Mixed alpha-beta]]
| + | |
| Structural highlights
Function
AMPD_CITFR Involved in both cell wall peptidoglycans recycling and beta-lactamase induction. Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
AmpD is a bacterial amidase involved in the recycling of cell-wall fragments in Gram-negative bacteria. Inactivation of AmpD leads to derepression of beta-lactamase expression, presenting a major pathway for the acquisition of constitutive antibiotic resistance. Here, we report the NMR structure of AmpD from Citrobacter freundii (PDB accession code 1J3G). A deep substrate-binding pocket explains the observed specificity for low molecular mass substrates. The fold is related to that of bacteriophage T7 lysozyme. Both proteins bind zinc at a conserved site and require zinc for amidase activity, although the enzymatic mechanism seems to differ in detail. The structure-based sequence alignment identifies conserved features that are also conserved in the eukaryotic peptidoglycan recognition protein (PGRP) domains, including the zinc-coordination site in several of them. PGRP domains thus belong to the same fold family and, where zinc-binding residues are conserved, may have amidase activity. This hypothesis is supported by the observation that human serum N-acetylmuramyl-L-alanine amidase seems to be identical with a soluble form of human PGRP-L.
NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme and homology with PGRP domains.,Liepinsh E, Genereux C, Dehareng D, Joris B, Otting G J Mol Biol. 2003 Apr 4;327(4):833-42. PMID:12654266[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liepinsh E, Genereux C, Dehareng D, Joris B, Otting G. NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme and homology with PGRP domains. J Mol Biol. 2003 Apr 4;327(4):833-42. PMID:12654266
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