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1lns

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(New page: 200px<br /><applet load="1lns" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lns, resolution 2.20&Aring;" /> '''Crystal Structure An...)
Current revision (07:34, 14 February 2024) (edit) (undo)
 
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[[Image:1lns.jpg|left|200px]]<br /><applet load="1lns" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lns, resolution 2.20&Aring;" />
 
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'''Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus lactis'''<br />
 
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==Overview==
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==Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus lactis==
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The X-prolyl dipeptidyl aminopeptidase (X-PDAP) from Lactococcus lactis is, a dimeric enzyme catalyzing the removal of Xaa-Pro dipeptides from the N, terminus of peptides. The structure of the enzyme was solved at 2.2 A, resolution and provides a model for the peptidase family S15. Each monomer, is composed of four domains. The larger one presents an alpha/beta, hydrolase fold and comprises the active site serine. The specificity, pocket is mainly built by residues from a small helical domain which is, together with the N-terminal domain, essential for dimerization. A, C-terminal moiety probably plays a role in the tropism of X-PDAP toward, the cellular membrane. These results give new insights for further, exploration of the role of the enzymes of the SC clan.
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<StructureSection load='1lns' size='340' side='right'caption='[[1lns]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1lns]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LNS FirstGlance]. <br>
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1LNS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Active as [http://en.wikipedia.org/wiki/Xaa-Pro_dipeptidyl-peptidase Xaa-Pro dipeptidyl-peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.11 3.4.14.11] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LNS OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lns OCA], [https://pdbe.org/1lns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lns RCSB], [https://www.ebi.ac.uk/pdbsum/1lns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lns ProSAT]</span></td></tr>
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==Reference==
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</table>
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The structural basis for catalysis and specificity of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis., Rigolet P, Mechin I, Delage MM, Chich JF, Structure. 2002 Oct;10(10):1383-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12377124 12377124]
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== Function ==
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[https://www.uniprot.org/uniprot/PEPX_LACLC PEPX_LACLC] Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.[HAMAP-Rule:MF_00698]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ln/1lns_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1lns ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Lactococcus lactis]]
[[Category: Lactococcus lactis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Xaa-Pro dipeptidyl-peptidase]]
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[[Category: Chich JF]]
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[[Category: Chich, J.F.]]
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[[Category: Delage MM]]
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[[Category: Delage, M.M.]]
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[[Category: Mechin I]]
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[[Category: Mechin, I.]]
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[[Category: Rigolet P]]
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[[Category: Rigolet, P.]]
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[[Category: alpha beta hydrolase fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:42:18 2007''
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Current revision

Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus lactis

PDB ID 1lns

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