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==PanDDA analysis group deposition -- Crystal Structure of Porphyromonas gingivalis in complex with Z321318226== | ==PanDDA analysis group deposition -- Crystal Structure of Porphyromonas gingivalis in complex with Z321318226== | ||
<StructureSection load='5sdl' size='340' side='right'caption='[[5sdl]]' scene=''> | <StructureSection load='5sdl' size='340' side='right'caption='[[5sdl]], [[Resolution|resolution]] 2.44Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SDL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SDL FirstGlance]. <br> | <table><tr><td colspan='2'>[[5sdl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Porphyromonas_gingivalis Porphyromonas gingivalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SDL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SDL FirstGlance]. <br> | ||
</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=5sdl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sdl OCA], [https://pdbe.org/5sdl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5sdl RCSB], [https://www.ebi.ac.uk/pdbsum/5sdl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5sdl ProSAT]</span></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]] 2.44Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=JHJ:N-(4-methoxyphenyl)-N-pyridin-4-ylurea'>JHJ</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=5sdl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sdl OCA], [https://pdbe.org/5sdl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5sdl RCSB], [https://www.ebi.ac.uk/pdbsum/5sdl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5sdl ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/DPP11_PORG3 DPP11_PORG3] Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Shows a strict specificity for acidic residues (Asp or Glu) in the P1 position, and has a hydrophobic residue preference at the P2 position. Preferentially cleaves the synthetic substrate Leu-Asp-methylcoumaryl-7-amide (Leu-Asp-MCA) as compared to Leu-Glu-MCA. Is involved in amino acid metabolism and bacterial growth of asaccharolytic P.gingivalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources.<ref>PMID:21896480</ref> <ref>PMID:23246913</ref> | |||
==See Also== | |||
*[[Dipeptidyl peptidase 3D structures|Dipeptidyl peptidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Porphyromonas gingivalis]] | |||
[[Category: Bezerra GA]] | [[Category: Bezerra GA]] | ||
[[Category: Bountra C]] | [[Category: Bountra C]] |
Revision as of 18:31, 6 March 2024
PanDDA analysis group deposition -- Crystal Structure of Porphyromonas gingivalis in complex with Z321318226PanDDA analysis group deposition -- Crystal Structure of Porphyromonas gingivalis in complex with Z321318226
Structural highlights
FunctionDPP11_PORG3 Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Shows a strict specificity for acidic residues (Asp or Glu) in the P1 position, and has a hydrophobic residue preference at the P2 position. Preferentially cleaves the synthetic substrate Leu-Asp-methylcoumaryl-7-amide (Leu-Asp-MCA) as compared to Leu-Glu-MCA. Is involved in amino acid metabolism and bacterial growth of asaccharolytic P.gingivalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources.[1] [2] See AlsoReferences
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