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| | ==Structure of EspG3 chaperone from the type VII (ESX-3) secretion system, space group P43212== | | ==Structure of EspG3 chaperone from the type VII (ESX-3) secretion system, space group P43212== |
| - | <StructureSection load='4rcl' size='340' side='right' caption='[[4rcl]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='4rcl' size='340' side='right'caption='[[4rcl]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4rcl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs2 Mycs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RCL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RCL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4rcl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RCL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RCL FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4l4w|4l4w]]</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]] 2.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MSMEG_0622, MSMEI_0606 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</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=4rcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rcl OCA], [https://pdbe.org/4rcl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rcl RCSB], [https://www.ebi.ac.uk/pdbsum/4rcl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rcl 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=4rcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rcl OCA], [http://pdbe.org/4rcl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rcl RCSB], [http://www.ebi.ac.uk/pdbsum/4rcl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rcl ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ESPG3_MYCS2 ESPG3_MYCS2] |
| | <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: Mycs2]] | + | [[Category: Large Structures]] |
| - | [[Category: Korotkov, K V]] | + | [[Category: Mycolicibacterium smegmatis MC2 155]] |
| - | [[Category: Chaperone]] | + | [[Category: Korotkov KV]] |
| - | [[Category: Esx-3]]
| + | |
| - | [[Category: Protein secretion]]
| + | |
| - | [[Category: Rv0289]]
| + | |
| - | [[Category: Type vii secretion system]]
| + | |
| Structural highlights
Function
ESPG3_MYCS2
Publication Abstract from PubMed
Type VII secretion systems (ESX) are responsible for transport of multiple proteins in mycobacteria. How different ESX systems achieve specific secretion of cognate substrates remains elusive. In the ESX systems, the cytoplasmic chaperone EspG forms complexes with heterodimeric PE-PPE substrates that are secreted from the cells or remain associated with the cell surface. Here we report the crystal structure of the EspG1 chaperone from the ESX-1 system determined using a fusion strategy with T4 lysozyme. EspG1 adopts a quasi 2-fold symmetric structure that consists of a central beta-sheet and two alpha-helical bundles. Additionally, we describe the structures of EspG3 chaperones from four different crystal forms. Alternate conformations of the putative PE-PPE binding site are revealed by comparison of the available EspG3 structures. Analysis of EspG1, EspG3 and EspG5 chaperones using small-angle X-ray scattering (SAXS) reveals that EspG1 and EspG3 chaperones form dimers in solution, which we observed in several of our crystal forms. Finally, we propose a model of the ESX-3 specific EspG3-PE5-PPE4 complex based on the SAXS analysis.
Structural Variability of EspG Chaperones from Mycobacterial ESX-1, ESX-3 and ESX-5 Type VII Secretion Systems.,Tuukkanen AT, Freire D, Chan S, Arbing MA, Reed RW, Evans TJ, Zenkeviciute G, Kim J, Kahng S, Sawaya MR, Chaton CT, Wilmanns M, Eisenberg D, Parret AHA, Korotkov KV J Mol Biol. 2018 Nov 9. pii: S0022-2836(18)30423-6. doi:, 10.1016/j.jmb.2018.11.003. PMID:30419243[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tuukkanen AT, Freire D, Chan S, Arbing MA, Reed RW, Evans TJ, Zenkeviciute G, Kim J, Kahng S, Sawaya MR, Chaton CT, Wilmanns M, Eisenberg D, Parret AHA, Korotkov KV. Structural Variability of EspG Chaperones from Mycobacterial ESX-1, ESX-3 and ESX-5 Type VII Secretion Systems. J Mol Biol. 2018 Nov 9. pii: S0022-2836(18)30423-6. doi:, 10.1016/j.jmb.2018.11.003. PMID:30419243 doi:http://dx.doi.org/10.1016/j.jmb.2018.11.003
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