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==Crystal structure of the catalytic domain of DapE protein from V.cholerea==
==Crystal structure of the catalytic domain of DapE protein from V.cholerea==
<StructureSection load='4onw' size='340' side='right' caption='[[4onw]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='4onw' size='340' side='right'caption='[[4onw]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4onw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibch Vibch]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3t68 3t68]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ONW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ONW FirstGlance]. <br>
<table><tr><td colspan='2'>[[4onw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_O1_biovar_El_Tor_str._N16961 Vibrio cholerae O1 biovar El Tor str. N16961]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3t68 3t68]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ONW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ONW FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BU1:1,4-BUTANEDIOL'>BU1</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BU1:1,4-BUTANEDIOL'>BU1</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3isz|3isz]]</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=4onw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4onw OCA], [https://pdbe.org/4onw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4onw RCSB], [https://www.ebi.ac.uk/pdbsum/4onw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4onw ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dapE, VC_2152 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinyl-diaminopimelate_desuccinylase Succinyl-diaminopimelate desuccinylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.18 3.5.1.18] </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=4onw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4onw OCA], [http://pdbe.org/4onw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4onw RCSB], [http://www.ebi.ac.uk/pdbsum/4onw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4onw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/DAPE_VIBCH DAPE_VIBCH]] Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls (By similarity).[HAMAP-Rule:MF_01690]  
[https://www.uniprot.org/uniprot/DAPE_VIBCH DAPE_VIBCH] Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls (By similarity).[HAMAP-Rule:MF_01690]
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Succinyl-diaminopimelate desuccinylase]]
[[Category: Large Structures]]
[[Category: Vibch]]
[[Category: Vibrio cholerae O1 biovar El Tor str. N16961]]
[[Category: Anderson, W F]]
[[Category: Anderson WF]]
[[Category: Structural genomic]]
[[Category: Gu M]]
[[Category: Gu, M]]
[[Category: Jedrzejczak R]]
[[Category: Jedrzejczak, R]]
[[Category: Joachimiak A]]
[[Category: Joachimiak, A]]
[[Category: Makowska-Grzyska M]]
[[Category: Makowska-Grzyska, M]]
[[Category: Nocek B]]
[[Category: Nocek, B]]
[[Category: Aminopeptidase]]
[[Category: Csgid]]
[[Category: Dape]]
[[Category: Hydrolase]]
[[Category: M20]]
[[Category: National institute of allergy and infectious disease]]
[[Category: Niaid]]
[[Category: Zn binding]]