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2y2d

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<StructureSection load='2y2d' size='340' side='right' caption='[[2y2d]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2y2d' size='340' side='right' caption='[[2y2d]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2y2d]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y2D OCA]. <br>
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<table><tr><td colspan='2'>[[2y2d]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y2D FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1j3g|1j3g]], [[2y2e|2y2e]], [[2y2c|2y2c]], [[2y28|2y28]], [[2y2b|2y2b]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1j3g|1j3g]], [[2y2e|2y2e]], [[2y2c|2y2c]], [[2y28|2y28]], [[2y2b|2y2b]]</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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/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>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2y2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y2d RCSB], [http://www.ebi.ac.uk/pdbsum/2y2d PDBsum]</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=2y2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y2d RCSB], [http://www.ebi.ac.uk/pdbsum/2y2d PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[http://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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Crystal Structures of Bacterial Peptidoglycan Amidase AmpD and an Unprecedented Activation Mechanism.,Carrasco-Lopez C, Rojas-Altuve A, Zhang W, Hesek D, Lee M, Barbe S, Andre I, Ferrer P, Silva-Martin N, Castro GR, Martinez-Ripoll M, Mobashery S, Hermoso JA J Biol Chem. 2011 Sep 9;286(36):31714-22. Epub 2011 Jul 20. PMID:21775432<ref>PMID:21775432</ref>
Crystal Structures of Bacterial Peptidoglycan Amidase AmpD and an Unprecedented Activation Mechanism.,Carrasco-Lopez C, Rojas-Altuve A, Zhang W, Hesek D, Lee M, Barbe S, Andre I, Ferrer P, Silva-Martin N, Castro GR, Martinez-Ripoll M, Mobashery S, Hermoso JA J Biol Chem. 2011 Sep 9;286(36):31714-22. Epub 2011 Jul 20. PMID:21775432<ref>PMID:21775432</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
== References ==
== References ==
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[[Category: Citrobacter freundii]]
[[Category: Citrobacter freundii]]
[[Category: N-acetylmuramoyl-L-alanine amidase]]
[[Category: N-acetylmuramoyl-L-alanine amidase]]
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[[Category: Andre, I.]]
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[[Category: Andre, I]]
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[[Category: Barbe, S.]]
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[[Category: Barbe, S]]
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[[Category: Carrasco-Lopez, C.]]
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[[Category: Carrasco-Lopez, C]]
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[[Category: Hermoso, J A.]]
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[[Category: Hermoso, J A]]
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[[Category: Hesek, D.]]
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[[Category: Hesek, D]]
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[[Category: Lee, M.]]
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[[Category: Lee, M]]
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[[Category: Martinez-Ripoll, M.]]
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[[Category: Martinez-Ripoll, M]]
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[[Category: Mobashery, S.]]
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[[Category: Mobashery, S]]
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[[Category: Rojas-Altuve, A.]]
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[[Category: Rojas-Altuve, A]]
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[[Category: Silva-Martin, N.]]
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[[Category: Silva-Martin, N]]
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[[Category: Zhang, W.]]
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[[Category: Zhang, W]]
[[Category: Activation mechanism]]
[[Category: Activation mechanism]]
[[Category: Amidase_2 family]]
[[Category: Amidase_2 family]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Peptidoglycan amidase]]
[[Category: Peptidoglycan amidase]]

Revision as of 16:01, 25 December 2014

CRYSTAL STRUCTURE OF AMPD HOLOENZYME

2y2d, resolution 2.00Å

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