1j3g: Difference between revisions

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{{Seed}}
[[Image:1j3g.png|left|200px]]


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==Solution structure of Citrobacter Freundii AmpD==
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<StructureSection load='1j3g' size='340' side='right'caption='[[1j3g]]' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=ZN:ZINC+ION'>ZN</scene></td></tr>
{{STRUCTURE_1j3g|  PDB=1j3g  |  SCENE=  }}
<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>
== 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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j3/1j3g_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1j3g ConSurf].
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== 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.


===Solution structure of Citrobacter Freundii AmpD===
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<ref>PMID:12654266</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
{{ABSTRACT_PUBMED_12654266}}
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</StructureSection>
==About this Structure==
1J3G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii]. This structure supersedes the now removed PDB entries  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].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/12654266 12654266]
[[Category: Citrobacter freundii]]
[[Category: Citrobacter freundii]]
[[Category: N-acetylmuramoyl-L-alanine amidase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[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: Mixed alpha-beta]]
 
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Retrieved from "https://proteopedia.org/1j3g"