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| | <StructureSection load='2a1l' size='340' side='right'caption='[[2a1l]], [[Resolution|resolution]] 2.18Å' scene=''> | | <StructureSection load='2a1l' size='340' side='right'caption='[[2a1l]], [[Resolution|resolution]] 2.18Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2a1l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A1L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2a1l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A1L FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCW:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PCW</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]] 2.18Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pitpnb ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCW:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PCW</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=2a1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a1l OCA], [https://pdbe.org/2a1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a1l RCSB], [https://www.ebi.ac.uk/pdbsum/2a1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a1l 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=2a1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a1l OCA], [https://pdbe.org/2a1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a1l RCSB], [https://www.ebi.ac.uk/pdbsum/2a1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a1l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PIPNB_RAT PIPNB_RAT]] Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes.
| + | [https://www.uniprot.org/uniprot/PIPNB_RAT PIPNB_RAT] Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Doan, C N]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Helmkamp, G M]] | + | [[Category: Doan CN]] |
| - | [[Category: Tremblay, J M]] | + | [[Category: Helmkamp GM]] |
| - | [[Category: Vordtriede, P B]] | + | [[Category: Tremblay JM]] |
| - | [[Category: Yoder, M D]] | + | [[Category: Vordtriede PB]] |
| - | [[Category: Lipid binding protein]] | + | [[Category: Yoder MD]] |
| Structural highlights
Function
PIPNB_RAT Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes.
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
Phosphatidylinositol transfer protein (PITP) is a ubiquitous eukaryotic protein that preferentially binds either phosphatidylinositol or phosphatidylcholine and catalyzes the exchange of these lipids between membranes. Mammalian cytosolic PITPs include the ubiquitously expressed PITPalpha and PITPbeta isoforms (269-270 residues). The crystal structure of rat PITPbeta complexed to dioleoylphosphatidylcholine was determined to 2.18 A resolution with molecular replacement using rat PITPalpha (77% sequence identify) as the phasing model. A structure comparison of the alpha and beta isoforms reveals minimal differences in protein conformation, differences in acyl conformation in the two isoforms, and remarkable conservation of solvent structure around the bound lipid. A comparison of transfer activity by human and rat PITPs, using small unilamellar vesicles with carefully controlled phospholipid composition, indicates that the beta isoforms have minimal differences in transfer preference between PtdIns and PtdCho when donor vesicles contain predominantly PtdCho. When PtdCho and PtdIns are present in equivalent concentrations in donor vesicles, PtdIns transfer occurs at approximately 3-fold the rate of PtdCho. The rat PITPbeta isoform clearly has the most diminished transfer rate of the four proteins studied. With the two rat isoforms, site-directed mutations of two locations within the lipid binding cavity that possess differing biochemical properties were characterized: I84alpha/F83beta and F225alpha/L224beta. The 225/224 locus is more critical in determining substrate specificity. Following the mutation of this locus to the other amino acid, the PtdCho transfer specific activity became PITPalpha (F225L) approximately PITPbeta and PITPbeta (L224F) approximately PITPalpha. The 225alpha/224beta locus plays a modest role in the specificity of both isoforms toward CerPCho.
Structure of PITPbeta in complex with phosphatidylcholine: comparison of structure and lipid transfer to other PITP isoforms.,Vordtriede PB, Doan CN, Tremblay JM, Helmkamp GM Jr, Yoder MD Biochemistry. 2005 Nov 15;44(45):14760-71. PMID:16274224[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Vordtriede PB, Doan CN, Tremblay JM, Helmkamp GM Jr, Yoder MD. Structure of PITPbeta in complex with phosphatidylcholine: comparison of structure and lipid transfer to other PITP isoforms. Biochemistry. 2005 Nov 15;44(45):14760-71. PMID:16274224 doi:10.1021/bi051191r
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