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==Structure of Transferase mutant-C23S,C199S==
==Structure of Transferase mutant-C23S,C199S==
<StructureSection load='5h63' size='340' side='right' caption='[[5h63]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
<StructureSection load='5h63' size='340' side='right'caption='[[5h63]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5h63]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H63 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H63 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5h63]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H63 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</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]] 1.92&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h5y|5h5y]], [[5h60|5h60]], [[5h61|5h61]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</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=5h63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h63 OCA], [http://pdbe.org/5h63 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h63 RCSB], [http://www.ebi.ac.uk/pdbsum/5h63 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h63 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=5h63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h63 OCA], [https://pdbe.org/5h63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h63 RCSB], [https://www.ebi.ac.uk/pdbsum/5h63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h63 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SSEK2_SALTY SSEK2_SALTY] Protein-arginine N-acetylglucosaminyltransferase effector that catalyzes the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins such as FADD: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions (PubMed:28522607). Also acts on host proteins without a death domain: catalyzes arginine GlcNAcylation of host small Rab1 GTPase, thereby preventing GTPase activity and leading to impaired host vesicular protein transport (By similarity). In contrast to Ssek1, not able to disrupt TNF signaling in infected cells (PubMed:28522607).[UniProtKB:P0DUJ8]<ref>PMID:28522607</ref>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Kim, J]]
[[Category: Large Structures]]
[[Category: Park, J B]]
[[Category: Kim J]]
[[Category: Yoo, Y]]
[[Category: Park JB]]
[[Category: Transferase]]
[[Category: Yoo Y]]

Latest revision as of 09:15, 20 March 2024

Structure of Transferase mutant-C23S,C199S

5h63, resolution 1.92Å

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