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| | <StructureSection load='4lya' size='340' side='right'caption='[[4lya]], [[Resolution|resolution]] 2.45Å' scene=''> | | <StructureSection load='4lya' size='340' side='right'caption='[[4lya]], [[Resolution|resolution]] 2.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4lya]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Geotn Geotn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LYA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LYA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4lya]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_thermodenitrificans_NG80-2 Geobacillus thermodenitrificans NG80-2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LYA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LYA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.45Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GTNG_0419 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=420246 GEOTN])</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=4lya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lya OCA], [https://pdbe.org/4lya PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lya RCSB], [https://www.ebi.ac.uk/pdbsum/4lya PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lya 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=4lya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lya OCA], [http://pdbe.org/4lya PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lya RCSB], [http://www.ebi.ac.uk/pdbsum/4lya PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lya ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ECCC_GEOTN ECCC_GEOTN] Part of the ESX specialized secretion system, which exports proteins from the cell including EsxA (ESAT-6) and EsxB (CFP-10) (By similarity). Might be the translocase subunit (PubMed:25865481). Probably only the first FtsK domain can hydrolyze ATP (PubMed:27130157).[UniProtKB:P9WNB1][UniProtKB:P9WNB3]<ref>PMID:25865481</ref> <ref>PMID:27130157</ref> |
| | <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: Geotn]] | + | [[Category: Geobacillus thermodenitrificans NG80-2]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bendebury, A]] | + | [[Category: Bendebury A]] |
| - | [[Category: Cox, J S]] | + | [[Category: Cox JS]] |
| - | [[Category: Dovala, D L]] | + | [[Category: Dovala DL]] |
| - | [[Category: Rosenberg, O S]] | + | [[Category: Rosenberg OS]] |
| - | [[Category: Stroud, R M]] | + | [[Category: Stroud RM]] |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Essc]]
| + | |
| - | [[Category: Esx secretion]]
| + | |
| - | [[Category: Type vii secretion]]
| + | |
| Structural highlights
Function
ECCC_GEOTN Part of the ESX specialized secretion system, which exports proteins from the cell including EsxA (ESAT-6) and EsxB (CFP-10) (By similarity). Might be the translocase subunit (PubMed:25865481). Probably only the first FtsK domain can hydrolyze ATP (PubMed:27130157).[UniProtKB:P9WNB1][UniProtKB:P9WNB3][1] [2]
Publication Abstract from PubMed
Mycobacterium tuberculosis and Staphylococcus aureus secrete virulence factors via type VII protein secretion (T7S), a system that intriguingly requires all of its secretion substrates for activity. To gain insights into T7S function, we used structural approaches to guide studies of the putative translocase EccC, a unique enzyme with three ATPase domains, and its secretion substrate EsxB. The crystal structure of EccC revealed that the ATPase domains are joined by linker/pocket interactions that modulate its enzymatic activity. EsxB binds via its signal sequence to an empty pocket on the C-terminal ATPase domain, which is accompanied by an increase in ATPase activity. Surprisingly, substrate binding does not activate EccC allosterically but, rather, by stimulating its multimerization. Thus, the EsxB substrate is also an integral T7S component, illuminating a mechanism that helps to explain interdependence of substrates, and suggests a model in which binding of substrates modulates their coordinate release from the bacterium.
Substrates Control Multimerization and Activation of the Multi-Domain ATPase Motor of Type VII Secretion.,Rosenberg OS, Dovala D, Li X, Connolly L, Bendebury A, Finer-Moore J, Holton J, Cheng Y, Stroud RM, Cox JS Cell. 2015 Apr 23;161(3):501-12. doi: 10.1016/j.cell.2015.03.040. Epub 2015 Apr, 9. PMID:25865481[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rosenberg OS, Dovala D, Li X, Connolly L, Bendebury A, Finer-Moore J, Holton J, Cheng Y, Stroud RM, Cox JS. Substrates Control Multimerization and Activation of the Multi-Domain ATPase Motor of Type VII Secretion. Cell. 2015 Apr 23;161(3):501-12. doi: 10.1016/j.cell.2015.03.040. Epub 2015 Apr, 9. PMID:25865481 doi:http://dx.doi.org/10.1016/j.cell.2015.03.040
- ↑ Zoltner M, Ng WM, Money JJ, Fyfe PK, Kneuper H, Palmer T, Hunter WN. EssC: domain structures inform on the elusive translocation channel in the Type VII secretion system. Biochem J. 2016 Jul 1;473(13):1941-52. doi: 10.1042/BCJ20160257. Epub 2016 Apr, 29. PMID:27130157 doi:http://dx.doi.org/10.1042/BCJ20160257
- ↑ Rosenberg OS, Dovala D, Li X, Connolly L, Bendebury A, Finer-Moore J, Holton J, Cheng Y, Stroud RM, Cox JS. Substrates Control Multimerization and Activation of the Multi-Domain ATPase Motor of Type VII Secretion. Cell. 2015 Apr 23;161(3):501-12. doi: 10.1016/j.cell.2015.03.040. Epub 2015 Apr, 9. PMID:25865481 doi:http://dx.doi.org/10.1016/j.cell.2015.03.040
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