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| | <StructureSection load='6e8m' size='340' side='right'caption='[[6e8m]], [[Resolution|resolution]] 1.61Å' scene=''> | | <StructureSection load='6e8m' size='340' side='right'caption='[[6e8m]], [[Resolution|resolution]] 1.61Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6e8m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Legln Legln]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E8M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E8M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6e8m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Legionella_longbeachae_NSW150 Legionella longbeachae NSW150]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E8M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E8M FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</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]] 1.61Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LLO_2327 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=661367 LEGLN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</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=6e8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e8m OCA], [http://pdbe.org/6e8m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e8m RCSB], [http://www.ebi.ac.uk/pdbsum/6e8m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e8m 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=6e8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e8m OCA], [https://pdbe.org/6e8m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e8m RCSB], [https://www.ebi.ac.uk/pdbsum/6e8m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e8m ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DNJA1_HUMAN DNJA1_HUMAN]] Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria. | + | [https://www.uniprot.org/uniprot/D3HJY4_LEGLN D3HJY4_LEGLN] |
| | <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: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Legln]] | + | [[Category: Legionella longbeachae NSW150]] |
| - | [[Category: Kaneko, T]] | + | [[Category: Kaneko T]] |
| - | [[Category: Li, S S.C]] | + | [[Category: Li SSC]] |
| - | [[Category: Peptide binding protein]]
| + | |
| - | [[Category: Src homology 2 domain]]
| + | |
| Structural highlights
Function
D3HJY4_LEGLN
Publication Abstract from PubMed
Src homology 2 (SH2) domains play a critical role in signal transduction in mammalian cells by binding to phosphorylated Tyr (pTyr). Apart from a few isolated cases in viruses, no functional SH2 domain has been identified to date in prokaryotes. Here we identify 93 SH2 domains from Legionella that are distinct in sequence and specificity from mammalian SH2 domains. The bacterial SH2 domains are not only capable of binding proteins or peptides in a Tyr phosphorylation-dependent manner, some bind pTyr itself with micromolar affinities, a property not observed for mammalian SH2 domains. The Legionella SH2 domains feature the SH2 fold and a pTyr-binding pocket, but lack a specificity pocket found in a typical mammalian SH2 domain for recognition of sequences flanking the pTyr residue. Our work expands the boundary of phosphotyrosine signalling to prokaryotes, suggesting that some bacterial effector proteins have acquired pTyr-superbinding characteristics to facilitate bacterium-host interactions.
Identification and characterization of a large family of superbinding bacterial SH2 domains.,Kaneko T, Stogios PJ, Ruan X, Voss C, Evdokimova E, Skarina T, Chung A, Liu X, Li L, Savchenko A, Ensminger AW, Li SS Nat Commun. 2018 Oct 31;9(1):4549. doi: 10.1038/s41467-018-06943-2. PMID:30382091[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kaneko T, Stogios PJ, Ruan X, Voss C, Evdokimova E, Skarina T, Chung A, Liu X, Li L, Savchenko A, Ensminger AW, Li SS. Identification and characterization of a large family of superbinding bacterial SH2 domains. Nat Commun. 2018 Oct 31;9(1):4549. doi: 10.1038/s41467-018-06943-2. PMID:30382091 doi:http://dx.doi.org/10.1038/s41467-018-06943-2
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