1lfw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:26, 13 March 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1lfw.gif|left|200px]]
 
-
{{Structure
+
==Crystal structure of pepV==
-
|PDB= 1lfw |SIZE=350|CAPTION= <scene name='initialview01'>1lfw</scene>, resolution 1.8&Aring;
+
<StructureSection load='1lfw' size='340' side='right'caption='[[1lfw]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=AEP:3-[(1-AMINO-2-CARBOXY-ETHYL)-HYDROXY-PHOSPHINOYL]-2-METHYL-PROPIONIC ACID'>AEP</scene>
+
<table><tr><td colspan='2'>[[1lfw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactobacillus_delbrueckii_subsp._lactis Lactobacillus delbrueckii subsp. lactis]. 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>
-
|ACTIVITY= [http://en.wikipedia.org/wiki/Xaa-His_dipeptidase Xaa-His dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.3 3.4.13.3]
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-
|GENE=
+
<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='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>
-
'''Crystal structure of pepV'''
+
== Function ==
-
 
+
[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 ==
-
==Overview==
+
[[Image:Consurf_key_small.gif|200px|right]]
-
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.
+
Check<jmol>
-
 
+
<jmolCheckbox>
-
==About this Structure==
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lf/1lfw_consurf.spt"</scriptWhenChecked>
-
1LFW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LFW OCA].
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
 
+
<text>to colour the structure by Evolutionary Conservation</text>
-
==Reference==
+
</jmolCheckbox>
-
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:[http://www.ncbi.nlm.nih.gov/pubmed/12176387 12176387]
+
</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=1lfw ConSurf].
-
[[Category: ]]
+
<div style="clear:both"></div>
-
[[Category: Single protein]]
+
== References ==
-
[[Category: Xaa-His dipeptidase]]
+
<references/>
-
[[Category: Bartunik, H.]]
+
__TOC__
-
[[Category: Bode, W.]]
+
</StructureSection>
-
[[Category: Bourenkow, G.]]
+
[[Category: Lactobacillus delbrueckii subsp. lactis]]
-
[[Category: Dive, V.]]
+
[[Category: Large Structures]]
-
[[Category: Henrich, B.]]
+
[[Category: Bartunik H]]
-
[[Category: Huber, R.]]
+
[[Category: Bode W]]
-
[[Category: Jozic, D.]]
+
[[Category: Bourenkow G]]
-
[[Category: Maskos, K.]]
+
[[Category: Dive V]]
-
[[Category: Scholze, H.]]
+
[[Category: Henrich B]]
-
[[Category: AEP]]
+
[[Category: Huber R]]
-
[[Category: ZN]]
+
[[Category: Jozic D]]
-
[[Category: dipeptidase]]
+
[[Category: Maskos K]]
-
[[Category: hydrolase]]
+
[[Category: Scholze H]]
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:30:27 2008''
+

Current revision

Crystal structure of pepV

PDB ID 1lfw

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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