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5mse

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==GFP Nuclear Transport Receptor Mutant==
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==GFP nuclear transport receptor mimic 3B8==
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<StructureSection load='5mse' size='340' side='right' caption='[[5mse]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
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<StructureSection load='5mse' size='340' side='right'caption='[[5mse]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5mse]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MSE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MSE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5mse]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MSE FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.66&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<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=5mse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mse OCA], [http://pdbe.org/5mse PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mse RCSB], [http://www.ebi.ac.uk/pdbsum/5mse PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mse ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5mse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mse OCA], [https://pdbe.org/5mse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mse RCSB], [https://www.ebi.ac.uk/pdbsum/5mse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mse ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI]] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
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[https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Nuclear pore complexes (NPCs) conduct nucleocytoplasmic transport through an FG domain-controlled barrier. We now explore how surface-features of a mobile species determine its NPC passage rate. Negative charges and lysines impede passage. Hydrophobic residues, certain polar residues (Cys, His), and, surprisingly, charged arginines have striking translocation-promoting effects. Favorable cation-pi interactions between arginines and FG-phenylalanines may explain this apparent paradox. Application of these principles to redesign the surface of GFP resulted in variants that show a wide span of transit rates, ranging from 35-fold slower than wild-type to approximately 500 times faster, with the latter outpacing even naturally occurring nuclear transport receptors (NTRs). The structure of a fast and particularly FG-specific GFP(NTR) variant illustrates how NTRs can expose multiple regions for binding hydrophobic FG motifs while evading non-specific aggregation. Finally, we document that even for NTR-mediated transport, the surface-properties of the "passively carried" cargo can strikingly affect the translocation rate.
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Surface Properties Determining Passage Rates of Proteins through Nuclear Pores.,Frey S, Rees R, Schunemann J, Ng SC, Funfgeld K, Huyton T, Gorlich D Cell. 2018 Jun 28;174(1):202-217.e9. doi: 10.1016/j.cell.2018.05.045. PMID:29958108<ref>PMID:29958108</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5mse" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Gorlich, D]]
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[[Category: Aequorea victoria]]
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[[Category: Huyton, T]]
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[[Category: Large Structures]]
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[[Category: Fluorescent protein]]
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[[Category: Gorlich D]]
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[[Category: Gfp nuclear transport receptor]]
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[[Category: Huyton T]]

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GFP nuclear transport receptor mimic 3B8

PDB ID 5mse

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