6k2d

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<StructureSection load='6k2d' size='340' side='right'caption='[[6k2d]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
<StructureSection load='6k2d' size='340' side='right'caption='[[6k2d]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6k2d]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K2D FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6k2d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K2D FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27] </span></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]] 3.6&#8491;</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=6k2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k2d OCA], [http://pdbe.org/6k2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k2d RCSB], [http://www.ebi.ac.uk/pdbsum/6k2d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k2d 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=6k2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k2d OCA], [https://pdbe.org/6k2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k2d RCSB], [https://www.ebi.ac.uk/pdbsum/6k2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k2d ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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> [[http://www.uniprot.org/uniprot/IPA9_SHIFL IPA9_SHIFL]] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway and modulates the acute inflammatory responses, thus facilitating bacterial colonization within the host cell. Interacts with IKBKG (NEMO) and TNIP1 (ABIN-1), an ubiquitin-binding adapter protein, which results in TNIP1-dependent 'Lys-27'-linked polyubiquitination of IKBKG. Consequently, polyubiquitinated IKBKG undergoes proteasome-dependent degradation, which perturbs NF-kappa-B activation during bacterial infection. Uses UBE2D2 (UBCH5B) as an E2 ubiquitin-conjugating enzyme.<ref>PMID:15950937</ref> <ref>PMID:18005683</ref> <ref>PMID:20010814</ref>
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[https://www.uniprot.org/uniprot/IPA9_SHIFL IPA9_SHIFL] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway and modulates the acute inflammatory responses, thus facilitating bacterial colonization within the host cell. Interacts with IKBKG (NEMO) and TNIP1 (ABIN-1), an ubiquitin-binding adapter protein, which results in TNIP1-dependent 'Lys-27'-linked polyubiquitination of IKBKG. Consequently, polyubiquitinated IKBKG undergoes proteasome-dependent degradation, which perturbs NF-kappa-B activation during bacterial infection. Uses UBE2D2 (UBCH5B) as an E2 ubiquitin-conjugating enzyme.<ref>PMID:15950937</ref> <ref>PMID:18005683</ref> <ref>PMID:20010814</ref>
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==See Also==
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*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: RING-type E3 ubiquitin transferase]]
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[[Category: Shigella flexneri]]
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[[Category: Ji, C G]]
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[[Category: Ji CG]]
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[[Category: Xiao, J Y]]
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[[Category: Xiao JY]]
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[[Category: Complex]]
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[[Category: Hydrolase-transferase complex]]
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Current revision

The crystal structure of GBP1 with LRR domain of IpaH9.8

PDB ID 6k2d

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