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| | <StructureSection load='6k1z' size='340' side='right'caption='[[6k1z]], [[Resolution|resolution]] 2.31Å' scene=''> | | <StructureSection load='6k1z' size='340' side='right'caption='[[6k1z]], [[Resolution|resolution]] 2.31Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6k1z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K1Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K1Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6k1z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K1Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K1Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAR:FARNESYL'>FAR</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]] 2.307Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GBP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAR:FARNESYL'>FAR</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=6k1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k1z OCA], [http://pdbe.org/6k1z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k1z RCSB], [http://www.ebi.ac.uk/pdbsum/6k1z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k1z 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=6k1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k1z OCA], [https://pdbe.org/6k1z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k1z RCSB], [https://www.ebi.ac.uk/pdbsum/6k1z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k1z ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GBP1_HUMAN GBP1_HUMAN]] Hydrolyzes GTP to GMP in two consecutive cleavage reactions. Exhibits antiviral activity against influenza virus. Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes.<ref>PMID:22106366</ref> | + | [https://www.uniprot.org/uniprot/GBP1_HUMAN GBP1_HUMAN] Hydrolyzes GTP to GMP in two consecutive cleavage reactions. Exhibits antiviral activity against influenza virus. Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes.<ref>PMID:22106366</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6k1z" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6k1z" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Du, S]] | + | [[Category: Du S]] |
| - | [[Category: Xiao, J Y]] | + | [[Category: Xiao JY]] |
| - | [[Category: Gbp farnesylation]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
GBP1_HUMAN Hydrolyzes GTP to GMP in two consecutive cleavage reactions. Exhibits antiviral activity against influenza virus. Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes.[1]
Publication Abstract from PubMed
The guanylate-binding proteins (GBPs) belong to the dynamin superfamily of GTPases and function in cell-autonomous defense against intracellular pathogens. IpaH9.8, an E3 ligase from the pathogenic bacterium Shigella flexneri, ubiquitinates a subset of GBPs and leads to their proteasomal degradation. Here we report the structure of a C-terminally truncated GBP1 in complex with the IpaH9.8 Leucine-rich repeat (LRR) domain. IpaH9.8LRR engages the GTPase domain of GBP1, and differences in the Switch II and alpha3 helix regions render some GBPs such as GBP3 and GBP7 resistant to IpaH9.8. Comparisons with other IpaH structures uncover interaction hot spots in their LRR domains. The C-terminal region of GBP1 undergoes a large rotation compared to previously determined structures. We further show that the C-terminal farnesylation modification also plays a role in regulating GBP1 conformation. Our results suggest a general mechanism by which the IpaH proteins target their cellular substrates and shed light on the structural dynamics of the GBPs.
Structural mechanism for guanylate-binding proteins (GBPs) targeting by the Shigella E3 ligase IpaH9.8.,Ji C, Du S, Li P, Zhu Q, Yang X, Long C, Yu J, Shao F, Xiao J PLoS Pathog. 2019 Jun 19;15(6):e1007876. doi: 10.1371/journal.ppat.1007876., eCollection 2019 Jun. PMID:31216343[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nordmann A, Wixler L, Boergeling Y, Wixler V, Ludwig S. A new splice variant of the human guanylate-binding protein 3 mediates anti-influenza activity through inhibition of viral transcription and replication. FASEB J. 2012 Mar;26(3):1290-300. doi: 10.1096/fj.11-189886. Epub 2011 Nov 21. PMID:22106366 doi:http://dx.doi.org/10.1096/fj.11-189886
- ↑ Ji C, Du S, Li P, Zhu Q, Yang X, Long C, Yu J, Shao F, Xiao J. Structural mechanism for guanylate-binding proteins (GBPs) targeting by the Shigella E3 ligase IpaH9.8. PLoS Pathog. 2019 Jun 19;15(6):e1007876. doi: 10.1371/journal.ppat.1007876., eCollection 2019 Jun. PMID:31216343 doi:http://dx.doi.org/10.1371/journal.ppat.1007876
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