6hv6
From Proteopedia
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<StructureSection load='6hv6' size='340' side='right'caption='[[6hv6]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='6hv6' size='340' side='right'caption='[[6hv6]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6hv6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[6hv6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Photorhabdus_asymbiotica_subsp._asymbiotica_ATCC_43949 Photorhabdus asymbiotica subsp. asymbiotica ATCC 43949]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HV6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HV6 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAU_02230 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=553480 PHOAA])</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=6hv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hv6 OCA], [https://pdbe.org/6hv6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hv6 RCSB], [https://www.ebi.ac.uk/pdbsum/6hv6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hv6 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=6hv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hv6 OCA], [https://pdbe.org/6hv6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hv6 RCSB], [https://www.ebi.ac.uk/pdbsum/6hv6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hv6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[https://www.uniprot.org/uniprot/PATOX_PHOAA PATOX_PHOAA]] Toxin that acts on host cells by modifying Rho proteins by tyrosine GlcNAcylation and heterotrimeric G alpha proteins by deamidation. Catalyzes the mono-O-GlcNAcylation of small GTPases of the Rho family (RhoA, RhoB, RhoC, Rac1, Rac2, Rac3, Cdc42) in eukaryotic host cells at the conserved tyrosine residue located in the switch I region (Tyr-32/34), using UDP-N-acetylglucosamine (UDP-GlcNAc) as the sugar donor; other GTPases of the Rho, Ras or Rab families are not substrates. Tyrosine glycosylation inhibits Rho activation and prevents interaction with downstream effectors, resulting in actin disassembly, inhibition of phagocytosis, cell rounding, and toxicity toward insects and mammalian cells. Also catalyzes the deamidation of the catalytic glutamine in heterotrimeric G alpha proteins (Gi, Gq/11), which blocks GTP hydrolysis and arrests the G proteins in a permanent active state leading to activation of Rho GTPases. Thus, PaTox hijacks host GTPase signaling in a bidirectional manner by deamidation-induced activation and glycosylation-induced inactivation of GTPases.<ref>PMID:24141704</ref> | + | [[https://www.uniprot.org/uniprot/PATOX_PHOAA PATOX_PHOAA]] Toxin that acts on host cells by modifying Rho proteins by tyrosine GlcNAcylation and heterotrimeric G alpha proteins by deamidation. Catalyzes the mono-O-GlcNAcylation of small GTPases of the Rho family (RhoA, RhoB, RhoC, Rac1, Rac2, Rac3, Cdc42) in eukaryotic host cells at the conserved tyrosine residue located in the switch I region (Tyr-32/34), using UDP-N-acetylglucosamine (UDP-GlcNAc) as the sugar donor; other GTPases of the Rho, Ras or Rab families are not substrates. Tyrosine glycosylation inhibits Rho activation and prevents interaction with downstream effectors, resulting in actin disassembly, inhibition of phagocytosis, cell rounding, and toxicity toward insects and mammalian cells. Also catalyzes the deamidation of the catalytic glutamine in heterotrimeric G alpha proteins (Gi, Gq/11), which blocks GTP hydrolysis and arrests the G proteins in a permanent active state leading to activation of Rho GTPases. Thus, PaTox hijacks host GTPase signaling in a bidirectional manner by deamidation-induced activation and glycosylation-induced inactivation of GTPases.<ref>PMID:24141704</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Photorhabdus asymbiotica subsp. asymbiotica ATCC 43949]] |
| - | [[Category: Bogdanovic | + | [[Category: Bogdanovic X]] |
| - | [[Category: Hunte | + | [[Category: Hunte C]] |
| - | [[Category: Wirth | + | [[Category: Wirth C]] |
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Revision as of 06:19, 8 September 2022
Crystal structure of PatoxP, a cysteine protease-like domain of Photorhabdus asymbiotica toxin PaTox
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