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{{STRUCTURE_4bwc|  PDB=4bwc  |  SCENE=  }}
==X-ray structure of a phospholiapse B like protein 1 from bovine kidneys==
===X-ray structure of a phospholiapse B like protein 1 from bovine kidneys===
<StructureSection load='4bwc' size='340' side='right' caption='[[4bwc]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
{{ABSTRACT_PUBMED_23934913}}
== Structural highlights ==
<table><tr><td colspan='2'>[[4bwc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BWC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BWC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=P4G:1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE'>P4G</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></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=4bwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bwc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bwc RCSB], [http://www.ebi.ac.uk/pdbsum/4bwc PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The main function of lysosomal proteins is to degrade cellular macromolecules. We purified a novel lysosomal protein to homogeneity from bovine kidneys. By gene annotation this protein is defined as a phospholipase B-like protein 1 (bPLBD1) and, to better understand its biological function, we solved its structure at 1.9 A resolution. We showed that bPLBD1 has uniform non-complex type N-glycosylation and that it localised to the lysosome. The first step in lysosomal protein transport, the initiation of mannose-6-phosphorylation by a N-acetylglucosamine-1-phosphotransferase, requires recognition of at least two distinct lysines on the protein surface. We identified candidate lysines by analysing the structural and sequentially conserved N-glycosylation sites and lysines in bPLBD1 and in the homologous mouse phospholipase B-like protein 2. Our model suggests that N408 is the primarily phosphorylated glycan, and K358 a key residue for N-acetylglucosamine-1-phosphotransferase recognition. Two other lysines, K334 and K342, provide the required second site for N-acetylglucosamine-1-phosphotransferase recognition. bPLBD1 is an N-terminal nucleophile (Ntn) hydrolase. By comparison with other Ntn-hydrolases, we conclude that the acyl moiety of PLBD1 substrate must be small to fit the putative binding pocket, while the space for the rest of the substrate is a large open cleft. Finally, as all the known substrates of Ntn-hydrolases have amide bonds, we suggest that bPLBD1 may be an amidase or peptidase instead of lipase, explaining the difficulty in finding a good substrate for any members of the PLBD family. (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc.


==Function==
Is the Bovine lysosomal phospholipase B-like protein an amidase?,Repo H, Kuokkanen E, Oksanen E, Goldman A, Heikinheimo P Proteins. 2013 Aug 12. doi: 10.1002/prot.24388. PMID:23934913<ref>PMID:23934913</ref>
[[http://www.uniprot.org/uniprot/PLBL1_BOVIN PLBL1_BOVIN]] Phospholipase acting on various phospholipids including phosphatidylcholine, phosphatidylinositol, phosphatidylethanolamine and lysophospholipids. May have a role in the defense against invading microorganisms and in the generation of lipid mediators of inflammation (By similarity).


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[4bwc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BWC OCA].
</div>
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:023934913</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Goldman, A.]]
[[Category: Goldman, A]]
[[Category: Heikinheimo, P.]]
[[Category: Heikinheimo, P]]
[[Category: Kuokkanen, E.]]
[[Category: Kuokkanen, E]]
[[Category: Oksanen, E.]]
[[Category: Oksanen, E]]
[[Category: Repo, H.]]
[[Category: Repo, H]]
[[Category: Glycosylation]]
[[Category: Glycosylation]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Lysosomal storage disorder]]
[[Category: Lysosomal storage disorder]]
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