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| | <StructureSection load='3eu5' size='340' side='right'caption='[[3eu5]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='3eu5' size='340' side='right'caption='[[3eu5]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3eu5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EU5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3EU5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3eu5]] is a 2 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=3EU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EU5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GBO:(2E,6E)-3,7-DIMETHYL-8-({5-[(3AS,4S,6AR)-2-OXOHEXAHYDRO-1H-THIENO[3,4-D]IMIDAZOL-4-YL]PENTANOYL}AMINO)OCTA-2,6-DIEN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>GBO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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">[[3euv|3euv]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GBO:(2E,6E)-3,7-DIMETHYL-8-({5-[(3AS,4S,6AR)-2-OXOHEXAHYDRO-1H-THIENO[3,4-D]IMIDAZOL-4-YL]PENTANOYL}AMINO)OCTA-2,6-DIEN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>GBO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_farnesyltransferase Protein farnesyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.58 2.5.1.58] </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=3eu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eu5 OCA], [https://pdbe.org/3eu5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eu5 RCSB], [https://www.ebi.ac.uk/pdbsum/3eu5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eu5 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3eu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eu5 OCA], [http://pdbe.org/3eu5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3eu5 RCSB], [http://www.ebi.ac.uk/pdbsum/3eu5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3eu5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FNTA_RAT FNTA_RAT]] Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate. Through RAC1 prenylation and activation may positively regulate neuromuscular junction development downstream of MUSK (By similarity). [[http://www.uniprot.org/uniprot/FNTB_RAT FNTB_RAT]] Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding. | + | [https://www.uniprot.org/uniprot/FNTA_RAT FNTA_RAT] Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate. Through RAC1 prenylation and activation may positively regulate neuromuscular junction development downstream of MUSK (By similarity). |
| | == 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: Protein farnesyltransferase]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Alexandrov, K]] | + | [[Category: Alexandrov K]] |
| - | [[Category: Blankenfeldt, W]] | + | [[Category: Blankenfeldt W]] |
| - | [[Category: Bon, R S]] | + | [[Category: Bon RS]] |
| - | [[Category: Delon, C]] | + | [[Category: Delon C]] |
| - | [[Category: Goody, R S]] | + | [[Category: Goody RS]] |
| - | [[Category: Guo, Z]] | + | [[Category: Guo Z]] |
| - | [[Category: Nguyen, U T.T]] | + | [[Category: Nguyen UTT]] |
| - | [[Category: Waldmann, H]] | + | [[Category: Waldmann H]] |
| - | [[Category: Wolters, D]] | + | [[Category: Wolters D]] |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Prenylome analysis]]
| + | |
| - | [[Category: Prenyltransferase]]
| + | |
| - | [[Category: Protein prenylation]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Zinc]]
| + | |
| Structural highlights
Function
FNTA_RAT Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate. Through RAC1 prenylation and activation may positively regulate neuromuscular junction development downstream of MUSK (By similarity).
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
Protein prenylation is a widespread phenomenon in eukaryotic cells that affects many important signaling molecules. We describe the structure-guided design of engineered protein prenyltransferases and their universal synthetic substrate, biotin-geranylpyrophosphate. These new tools allowed us to detect femtomolar amounts of prenylatable proteins in cells and organs and to identify their cognate protein prenyltransferases. Using this approach, we analyzed the in vivo effects of protein prenyltransferase inhibitors. Whereas some of the inhibitors displayed the expected activities, others lacked in vivo activity or targeted a broader spectrum of prenyltransferases than previously believed. To quantitate the in vivo effect of the prenylation inhibitors, we profiled biotin-geranyl-tagged RabGTPases across the proteome by mass spectrometry. We also demonstrate that sites of active vesicular transport carry most of the RabGTPases. This approach enables a quantitative proteome-wide analysis of the regulation of protein prenylation and its modulation by therapeutic agents.
Analysis of the eukaryotic prenylome by isoprenoid affinity tagging.,Nguyen UT, Guo Z, Delon C, Wu Y, Deraeve C, Franzel B, Bon RS, Blankenfeldt W, Goody RS, Waldmann H, Wolters D, Alexandrov K Nat Chem Biol. 2009 Apr;5(4):227-35. Epub 2009 Feb 15. PMID:19219049[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nguyen UT, Guo Z, Delon C, Wu Y, Deraeve C, Franzel B, Bon RS, Blankenfeldt W, Goody RS, Waldmann H, Wolters D, Alexandrov K. Analysis of the eukaryotic prenylome by isoprenoid affinity tagging. Nat Chem Biol. 2009 Apr;5(4):227-35. Epub 2009 Feb 15. PMID:19219049 doi:10.1038/nchembio.149
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