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1lfw

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Revision as of 06:43, 18 August 2021

Crystal structure of pepV

Structural highlights

1lfw is a 1 chain structure with sequence from "bacillus_lactis_acidi"_leichmann_1896 "bacillus lactis acidi" leichmann 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Activity:	Hydrolase, with EC number and 3.4.13.20 3.4.13.18 and 3.4.13.20
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PEPV_LACDL] Is a relatively unspecific dipeptidase cleaving a variety of dipeptides, notably those with an N-terminal beta-Ala or D-Ala residue, e.g. carnosine (beta-Ala-His). To a lesser extent, also shows aminopeptidase activity, since it is able to catalyze the removal of the N-terminal amino acid from a few distinct tripeptides.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

PepV from Lactobacillus delbrueckii, a dinuclear zinc peptidase, has been characterized as an unspecific amino dipeptidase. The crystal structure of PepV in complex with the phosphinic inhibitor AspPsi[PO(2)CH(2)]AlaOH, a dipeptide substrate mimetic, reveals a "catalytic domain" and a "lid domain," which together form an internal active site cavity that traps the inhibitor. The catalytic domain is topologically similar to catalytic domains from amino- and carboxypeptidases. However, the lid domain is unique among the related enzymes. In contrast to the other related exopeptidases, PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. The cocrystallized inhibitor illustrates the two roles of the two catalytic zinc ions, namely stabilization of the tetrahedral intermediate and activation of the catalytic water molecule.

Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides.,Jozic D, Bourenkow G, Bartunik H, Scholze H, Dive V, Henrich B, Huber R, Bode W, Maskos K Structure. 2002 Aug;10(8):1097-106. PMID:12176387^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Vongerichten KF, Klein JR, Matern H, Plapp R. Cloning and nucleotide sequence analysis of pepV, a carnosinase gene from Lactobacillus delbrueckii subsp. lactis DSM 7290, and partial characterization of the enzyme. Microbiology. 1994 Oct;140 ( Pt 10):2591-600. PMID:7528082
↑ Jozic D, Bourenkow G, Bartunik H, Scholze H, Dive V, Henrich B, Huber R, Bode W, Maskos K. Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides. Structure. 2002 Aug;10(8):1097-106. PMID:12176387

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lfw"

@@ Line 3: / Line 3: @@
 <StructureSection load='1lfw' size='340' side='right'caption='[[1lfw]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1lfw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_lactis_acidi"_leichmann_1896 "bacillus lactis acidi" leichmann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LFW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LFW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1lfw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_lactis_acidi"_leichmann_1896 "bacillus lactis acidi" leichmann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LFW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AEP:3-[(1-AMINO-2-CARBOXY-ETHYL)-HYDROXY-PHOSPHINOYL]-2-METHYL-PROPIONIC+ACID'>AEP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AEP:3-[(1-AMINO-2-CARBOXY-ETHYL)-HYDROXY-PHOSPHINOYL]-2-METHYL-PROPIONIC+ACID'>AEP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.18 and 3.4.13.20 3.4.13.18 and 3.4.13.20] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.18 and 3.4.13.20 3.4.13.18 and 3.4.13.20] </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=1lfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lfw OCA], [http://pdbe.org/1lfw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lfw RCSB], [http://www.ebi.ac.uk/pdbsum/1lfw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lfw ProSAT]</span></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=1lfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lfw OCA], [https://pdbe.org/1lfw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lfw RCSB], [https://www.ebi.ac.uk/pdbsum/1lfw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lfw ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PEPV_LACDL PEPV_LACDL]] Is a relatively unspecific dipeptidase cleaving a variety of dipeptides, notably those with an N-terminal beta-Ala or D-Ala residue, e.g. carnosine (beta-Ala-His). To a lesser extent, also shows aminopeptidase activity, since it is able to catalyze the removal of the N-terminal amino acid from a few distinct tripeptides.<ref>PMID:7528082</ref>
+[[https://www.uniprot.org/uniprot/PEPV_LACDL PEPV_LACDL]] Is a relatively unspecific dipeptidase cleaving a variety of dipeptides, notably those with an N-terminal beta-Ala or D-Ala residue, e.g. carnosine (beta-Ala-His). To a lesser extent, also shows aminopeptidase activity, since it is able to catalyze the removal of the N-terminal amino acid from a few distinct tripeptides.<ref>PMID:7528082</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1lfw

From Proteopedia

Revision as of 06:43, 18 August 2021

Crystal structure of pepV

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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