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4q5h

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==Shigella Effector Kinase OspG bound to AMPPNP and E2-Ub UbcH7-Ub Conjugate==
==Shigella Effector Kinase OspG bound to AMPPNP and E2-Ub UbcH7-Ub Conjugate==
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<StructureSection load='4q5h' size='340' side='right' caption='[[4q5h]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='4q5h' size='340' side='right'caption='[[4q5h]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4q5h]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q5H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q5H FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4q5h]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Shigella_sonnei_Ss046 Shigella sonnei Ss046]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q5H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q5H FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 1.999&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qse|4qse]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </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=4q5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q5h OCA], [https://pdbe.org/4q5h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q5h RCSB], [https://www.ebi.ac.uk/pdbsum/4q5h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q5h ProSAT]</span></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=4q5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q5h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q5h RCSB], [http://www.ebi.ac.uk/pdbsum/4q5h PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/OSPG_SHISS OSPG_SHISS]] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is a kinase that is involved in down-regulation of the host innate response induced by invasive bacteria (By similarity). [[http://www.uniprot.org/uniprot/UB2L3_HUMAN UB2L3_HUMAN]] Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis.<ref>PMID:10888878</ref> <ref>PMID:15367689</ref> <ref>PMID:17003263</ref> <ref>PMID:19340006</ref> <ref>PMID:18946090</ref> <ref>PMID:20061386</ref> <ref>PMID:21532592</ref> [[http://www.uniprot.org/uniprot/UBI4P_YEAST UBI4P_YEAST]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
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[https://www.uniprot.org/uniprot/OSPG_SHISS OSPG_SHISS] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is a kinase that is involved in down-regulation of the host innate response induced by invasive bacteria (By similarity).
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4q5h" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[3D structures of ubiquitin|3D structures of ubiquitin]]
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*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ubiquitin--protein ligase]]
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[[Category: Homo sapiens]]
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[[Category: Structural genomic]]
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[[Category: Large Structures]]
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[[Category: Cygler, M]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Grishin, A M]]
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[[Category: Shigella sonnei Ss046]]
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[[Category: Bsgi]]
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[[Category: Cygler M]]
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[[Category: Inhibition of nf-kb pathway]]
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[[Category: Grishin AM]]
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[[Category: Kinase fold]]
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[[Category: Protein binding]]
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[[Category: Protein-protein complex]]
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[[Category: Unknown function]]
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Current revision

Shigella Effector Kinase OspG bound to AMPPNP and E2-Ub UbcH7-Ub Conjugate

PDB ID 4q5h

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