View source for 6nff


==Structure of X-prolyl dipeptidyl aminopeptidase from Lactobacillus helveticus==
<StructureSection load='6nff' size='340' side='right'caption='[[6nff]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6nff]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactobacillus_helveticus Lactobacillus helveticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NFF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NFF FirstGlance]. <br>
</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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=6nff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nff OCA], [https://pdbe.org/6nff PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nff RCSB], [https://www.ebi.ac.uk/pdbsum/6nff PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nff ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PEPX_LACHE PEPX_LACHE] Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Prolyl aminodipeptidase (PepX) is an enzyme that hydrolyzes peptide bonds from the N-terminus of substrates when the penultimate amino-acid residue is a proline. Prolyl peptidases are of particular interest owing to their ability to hydrolyze food allergens that contain a high percentage of proline residues. PepX from Lactobacillus helveticus was cloned and expressed in Escherichia coli as an N-terminally His-tagged recombinant construct and was crystallized by hanging-drop vapor diffusion in a phosphate buffer using PEG 3350 as a precipitant. The structure was determined at 2.0 A resolution by molecular replacement using the structure of PepX from Lactococcus lactis (PDB entry 1lns) as the starting model. Notable differences between the L. helveticus PepX structure and PDB entry 1lns include a cysteine instead of a phenylalanine at the substrate-binding site in the position which confers exopeptidase activity and the presence of a calcium ion coordinated by a calcium-binding motif with the consensus sequence DX(DN)XDG.

Structural characterization of a prolyl aminodipeptidase (PepX) from Lactobacillus helveticus.,Ojennus DD, Bratt NJ, Jones KL, Juers DH Acta Crystallogr F Struct Biol Commun. 2019 Oct 1;75(Pt 10):625-633. doi:, 10.1107/S2053230X19011774. Epub 2019 Sep 20. PMID:31584010<ref>PMID:31584010</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6nff" style="background-color:#fffaf0;"></div>

==See Also==
*[[Dipeptidyl peptidase 3D structures|Dipeptidyl peptidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lactobacillus helveticus]]
[[Category: Large Structures]]
[[Category: Bratt NJ]]
[[Category: Juers DH]]
[[Category: Ojennus DD]]