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| | <StructureSection load='4n1a' size='340' side='right'caption='[[4n1a]], [[Resolution|resolution]] 3.24Å' scene=''> | | <StructureSection load='4n1a' size='340' side='right'caption='[[4n1a]], [[Resolution|resolution]] 3.24Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4n1a]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Thecd Thecd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N1A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N1A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4n1a]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermomonospora_curvata_DSM_43183 Thermomonospora curvata DSM 43183]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N1A 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='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></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tcur_0607 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=471852 THECD])</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=4n1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n1a OCA], [https://pdbe.org/4n1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n1a RCSB], [https://www.ebi.ac.uk/pdbsum/4n1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n1a 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=4n1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n1a OCA], [http://pdbe.org/4n1a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n1a RCSB], [http://www.ebi.ac.uk/pdbsum/4n1a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n1a ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ECCC_THECD ECCC_THECD] Part of the ESX specialized secretion system, which exports proteins from the cell including EsxA (ESAT-6) and EsxB (CFP-10) (PubMed:25865481). Has weak intrinsic ATPase activity; probably only the first FtsK domain can hydrolyze ATP (PubMed:25865481). Might be the translocase subunit (PubMed:25865481).<ref>PMID:25865481</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thecd]] | + | [[Category: Thermomonospora curvata DSM 43183]] |
| - | [[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: Atpase]]
| + | |
| - | [[Category: Protein binding-protein binding complex]]
| + | |
| Structural highlights
Function
ECCC_THECD Part of the ESX specialized secretion system, which exports proteins from the cell including EsxA (ESAT-6) and EsxB (CFP-10) (PubMed:25865481). Has weak intrinsic ATPase activity; probably only the first FtsK domain can hydrolyze ATP (PubMed:25865481). Might be the translocase subunit (PubMed:25865481).[1]
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[2]
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
- ↑ 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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