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| | <StructureSection load='3fgw' size='340' side='right'caption='[[3fgw]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='3fgw' size='340' side='right'caption='[[3fgw]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3fgw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FGW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3fgw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FGW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3fbx|3fbx]], [[3fgr|3fgr]], [[3fgt|3fgt]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AAG44101 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3fgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fgw OCA], [https://pdbe.org/3fgw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fgw RCSB], [https://www.ebi.ac.uk/pdbsum/3fgw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fgw 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=3fgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fgw OCA], [https://pdbe.org/3fgw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fgw RCSB], [https://www.ebi.ac.uk/pdbsum/3fgw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fgw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PLBL2_MOUSE PLBL2_MOUSE]] Putative phospholipase.
| + | [https://www.uniprot.org/uniprot/PLBL2_MOUSE PLBL2_MOUSE] Putative phospholipase. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Dickmanns, A]] | + | [[Category: Dickmanns A]] |
| - | [[Category: Ficner, R]] | + | [[Category: Ficner R]] |
| - | [[Category: Lakomek, K]] | + | [[Category: Lakomek K]] |
| - | [[Category: Alpha beta]]
| + | |
| - | [[Category: Disulphide bond]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Glycosylated]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Lipid degradation]]
| + | |
| - | [[Category: Lysosome]]
| + | |
| - | [[Category: N-terminal hydrolase fold]]
| + | |
| - | [[Category: Occupied pocket]]
| + | |
| - | [[Category: One chain form]]
| + | |
| Structural highlights
3fgw is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.8Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
PLBL2_MOUSE Putative phospholipase.
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
BACKGROUND: The lysosomal 66.3 kDa protein from mouse is a soluble, mannose 6-phosphate containing protein of so far unknown function. It is synthesized as a glycosylated 75 kDa precursor that undergoes limited proteolysis leading to a 28 kDa N- and a 40 kDa C-terminal fragment. RESULTS: In order to gain insight into the function and the post-translational maturation process of the glycosylated 66.3 kDa protein, three crystal structures were determined that represent different maturation states. These structures demonstrate that the 28 kDa and 40 kDa fragment which have been derived by a proteolytic cleavage remain associated. Mass spectrometric analysis confirmed the subsequent trimming of the C-terminus of the 28 kDa fragment making a large pocket accessible, at the bottom of which the putative active site is located. The crystal structures reveal a significant similarity of the 66.3 kDa protein to several bacterial hydrolases. The core alphabetabetaalpha sandwich fold and a cysteine residue at the N-terminus of the 40 kDa fragment (C249) classify the 66.3 kDa protein as a member of the structurally defined N-terminal nucleophile (Ntn) hydrolase superfamily. CONCLUSION: Due to the close resemblance of the 66.3 kDa protein to members of the Ntn hydrolase superfamily a hydrolytic activity on substrates containing a non-peptide amide bond seems reasonable. The structural homology which comprises both the overall fold and essential active site residues also implies an autocatalytic maturation process of the lysosomal 66.3 kDa protein. Upon the proteolytic cleavage between S248 and C249, a deep pocket becomes solvent accessible, which harbors the putative active site of the 66.3 kDa protein.
Initial insight into the function of the lysosomal 66.3 kDa protein from mouse by means of X-ray crystallography.,Lakomek K, Dickmanns A, Kettwig M, Urlaub H, Ficner R, Lubke T BMC Struct Biol. 2009 Aug 25;9:56. PMID:19706171[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lakomek K, Dickmanns A, Kettwig M, Urlaub H, Ficner R, Lubke T. Initial insight into the function of the lysosomal 66.3 kDa protein from mouse by means of X-ray crystallography. BMC Struct Biol. 2009 Aug 25;9:56. PMID:19706171 doi:10.1186/1472-6807-9-56
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