4nh0

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<StructureSection load='4nh0' size='340' side='right'caption='[[4nh0]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='4nh0' size='340' side='right'caption='[[4nh0]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4nh0]] is a 2 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=4NH0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NH0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4nh0]] is a 2 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=4NH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NH0 FirstGlance]. <br>
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</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<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>
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<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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=4nh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nh0 OCA], [http://pdbe.org/4nh0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nh0 RCSB], [http://www.ebi.ac.uk/pdbsum/4nh0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nh0 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nh0 OCA], [https://pdbe.org/4nh0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nh0 RCSB], [https://www.ebi.ac.uk/pdbsum/4nh0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nh0 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[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>
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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.
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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<ref>PMID:25865481</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4nh0" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Thecd]]
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[[Category: Thermomonospora curvata DSM 43183]]
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[[Category: Cox, J S]]
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[[Category: Cox JS]]
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[[Category: Dovala, D]]
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[[Category: Dovala D]]
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[[Category: Rosenberg, O S]]
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[[Category: Rosenberg OS]]
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[[Category: Strauli, N]]
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[[Category: Strauli N]]
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[[Category: Stroud, R M]]
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[[Category: Stroud RM]]
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[[Category: Atpase]]
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[[Category: Cell cycle]]
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[[Category: Esxb]]
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[[Category: Secretion]]
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Current revision

Cytoplasmic domain of the Thermomonospora curvata Type VII Secretion ATPase EccC

PDB ID 4nh0

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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