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| | ==Bacterial Effector NleH2 Kinase Domain== | | ==Bacterial Effector NleH2 Kinase Domain== |
| - | <StructureSection load='4lrk' size='340' side='right' caption='[[4lrk]], [[Resolution|resolution]] 2.27Å' scene=''> | + | <StructureSection load='4lrk' size='340' side='right'caption='[[4lrk]], [[Resolution|resolution]] 2.27Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4lrk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LRK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LRK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4lrk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LRK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LRK FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lrj|4lrj]]</td></tr> | + | </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=4lrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lrk OCA], [https://pdbe.org/4lrk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lrk RCSB], [https://www.ebi.ac.uk/pdbsum/4lrk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lrk ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECs1814, nleh2, Z6021 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</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/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=4lrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lrk OCA], [http://pdbe.org/4lrk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lrk RCSB], [http://www.ebi.ac.uk/pdbsum/4lrk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lrk ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8XAL6_ECO57 Q8XAL6_ECO57] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Eco57]] | + | [[Category: Escherichia coli O157:H7]] |
| - | [[Category: Non-specific serine/threonine protein kinase]]
| + | [[Category: Large Structures]] |
| - | [[Category: Structural genomic]] | + | [[Category: Cygler M]] |
| - | [[Category: Cygler, M]] | + | [[Category: Grishin AM]] |
| - | [[Category: Grishin, A M]] | + | |
| - | [[Category: Bacterial effector kinase]]
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| - | [[Category: Bsgi]]
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| - | [[Category: Kinase fold]]
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| - | [[Category: Transferase]]
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| Structural highlights
Function
Q8XAL6_ECO57
Publication Abstract from PubMed
Upon host cell infection, pathogenic Escherichia coli hijacks host cellular processes with the help of 20-60 secreted effector proteins that subvert cellular processes to create an environment conducive to bacterial survival. The NleH effector kinases manipulate the NF-kappaB pathway and prevent apoptosis. They show low sequence similarity to human regulatory kinases and contain two domains, the N-terminal, likely intrinsically unfolded, and a C-terminal kinase-like domain. We show that these effectors autophosphorylate on sites located predominantly in the N-terminal segment. The kinase domain displays a minimal kinase fold, but lacks an activation loop and the GHI subdomain. Nevertheless, all catalytically important residues are conserved. ATP binding proceeds with minimal structural rearrangements. The NleH structure is the first for the bacterial effector kinases family. NleHs and their homologous effector kinases form a new kinase family within the cluster of eukaryotic-like kinases that includes also Rio, Bud32, and KdoK families.
NleH Defines a New Family of Bacterial Effector Kinases.,Grishin AM, Cherney M, Anderson DH, Phanse S, Babu M, Cygler M Structure. 2013 Dec 24. pii: S0969-2126(13)00456-5. doi:, 10.1016/j.str.2013.11.006. PMID:24373767[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Grishin AM, Cherney M, Anderson DH, Phanse S, Babu M, Cygler M. NleH Defines a New Family of Bacterial Effector Kinases. Structure. 2013 Dec 24. pii: S0969-2126(13)00456-5. doi:, 10.1016/j.str.2013.11.006. PMID:24373767 doi:http://dx.doi.org/10.1016/j.str.2013.11.006
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