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| | <StructureSection load='4yk2' size='340' side='right'caption='[[4yk2]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='4yk2' size='340' side='right'caption='[[4yk2]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4yk2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Barc7 Barc7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YK2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YK2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4yk2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bartonella_clarridgeiae_73 Bartonella clarridgeiae 73]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YK2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.05Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yk1|4yk1]], [[4yk3|4yk3]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BARCL_1032 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=696125 BARC7])</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=4yk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yk2 OCA], [https://pdbe.org/4yk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yk2 RCSB], [https://www.ebi.ac.uk/pdbsum/4yk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yk2 ProSAT]</span></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=4yk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yk2 OCA], [http://pdbe.org/4yk2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yk2 RCSB], [http://www.ebi.ac.uk/pdbsum/4yk2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yk2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/E6YIM5_BARC7 E6YIM5_BARC7] |
| | <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: Barc7]] | + | [[Category: Bartonella clarridgeiae 73]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Structural genomic]] | |
| - | [[Category: Bartonella clarridgeiae]] | |
| - | [[Category: Bep9]] | |
| - | [[Category: Bid domain]] | |
| - | [[Category: Protein binding]] | |
| - | [[Category: Ssgcid]] | |
| - | [[Category: Virb-translocated bartonella effector protein]] | |
| Structural highlights
Function
E6YIM5_BARC7
Publication Abstract from PubMed
The BID (Bep intracellular delivery) domain functions as secretion signal in a subfamily of protein substrates of bacterial type IV secretion (T4S) systems. It mediates transfer of (1) relaxases and the attached DNA during bacterial conjugation, and (2) numerous Bartonella effector proteins (Beps) during protein transfer into host cells infected by pathogenic Bartonella species. Furthermore, BID domains of Beps have often evolved secondary effector functions within host cells. Here, we provide crystal structures for three representative BID domains and describe a novel conserved fold characterized by a compact, antiparallel four-helix bundle topped with a hook. The conserved hydrophobic core provides a rigid scaffold to a surface that, despite a few conserved exposed residues and similarities in charge distribution, displays significant variability. We propose that the genuine function of BID domains as T4S signal may primarily depend on their rigid structure, while the plasticity of their surface may facilitate adaptation to secondary effector functions.
The BID Domain of Type IV Secretion Substrates Forms a Conserved Four-Helix Bundle Topped with a Hook.,Stanger FV, de Beer TA, Dranow DM, Schirmer T, Phan I, Dehio C Structure. 2017 Jan 3;25(1):203-211. doi: 10.1016/j.str.2016.10.010. Epub 2016, Nov 23. PMID:27889208[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stanger FV, de Beer TA, Dranow DM, Schirmer T, Phan I, Dehio C. The BID Domain of Type IV Secretion Substrates Forms a Conserved Four-Helix Bundle Topped with a Hook. Structure. 2017 Jan 3;25(1):203-211. doi: 10.1016/j.str.2016.10.010. Epub 2016, Nov 23. PMID:27889208 doi:http://dx.doi.org/10.1016/j.str.2016.10.010
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