4ann: Difference between revisions
New page: '''Unreleased structure''' The entry 4ann is ON HOLD Authors: Zoltner, M., Fyfe, P., Palmer, T., Hunter, W.N. Description: Crystal Structure Staphylococcus aureus BOB cytoplasmic fragm... |
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The | ==Crystal Structure Staphylococcus aureus ESSB cytoplasmic fragment== | ||
<StructureSection load='4ann' size='340' side='right'caption='[[4ann]], [[Resolution|resolution]] 1.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ann]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_NCTC_8325 Staphylococcus aureus subsp. aureus NCTC 8325]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ANN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ANN FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.05Å</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=4ann FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ann OCA], [https://pdbe.org/4ann PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ann RCSB], [https://www.ebi.ac.uk/pdbsum/4ann PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ann ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ESSB_STAA8 ESSB_STAA8] Component of the type VII secretion system (Ess) (Probable). Required for the secretion of EsxA and EsxB (By similarity).[UniProtKB:P0C053] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The type VII protein translocation/secretion system, unique to Gram-positive bacteria is a key virulence determinant in Staphylococcus aureus. We aim to characterise the architecture of this secretion machinery and now describe a study of S. aureus EssB, a 52-kDa bitopic membrane protein essential for secretion of the ESAT-6-family-proteins, the prototypic substrate of Type VII secretion. Full-length EssB was heterologously expressed in Escherichia coli, solubilised from the bacterial membrane, purified to homogeneity and shown to be dimeric. A C-terminal truncation, EssBC, and two soluble fragments termed EssB-N and EssB-C, predicted to occur on either side of the cytoplasmic membrane, have been successfully purified in recombinant form, characterised and together with the full-length protein used in crystallisation trials. EssB-N, the 25 kDa N-terminal cytoplasmic fragment, gave well-ordered crystals and we report the structure, determined by single-wavelength anomalous diffraction (SAD) targeting an SeMet derivative, refined to atomic (1.05 A) resolution. EssB-N is dimeric in solution but crystallises as a monomer and displays a fold composed of two globular domains separated by a cleft. The structure is related to that of Ser/Thr protein kinases and our study identifies that the type VII secretion system exploits and re-uses a stable modular entity and fold that has evolved to participate in protein-protein interactions in a similar fashion to the catalytically inert pseudokinases. | |||
Characterisation of Staphylococcus aureus EssB, an integral membrane component of the Type VII secretion system; atomic resolution crystal structure of the cytoplasmic segment.,Zoltner M, Fyfe PK, Palmer T, Hunter WN Biochem J. 2012 Oct 25. PMID:23098276<ref>PMID:23098276</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4ann" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Staphylococcus aureus subsp. aureus NCTC 8325]] | |||
[[Category: Fyfe PK]] | |||
[[Category: Hunter WN]] | |||
[[Category: Palmer T]] | |||
[[Category: Zoltner M]] | |||
Latest revision as of 13:52, 9 May 2024
Crystal Structure Staphylococcus aureus ESSB cytoplasmic fragmentCrystal Structure Staphylococcus aureus ESSB cytoplasmic fragment
Structural highlights
FunctionESSB_STAA8 Component of the type VII secretion system (Ess) (Probable). Required for the secretion of EsxA and EsxB (By similarity).[UniProtKB:P0C053] Publication Abstract from PubMedThe type VII protein translocation/secretion system, unique to Gram-positive bacteria is a key virulence determinant in Staphylococcus aureus. We aim to characterise the architecture of this secretion machinery and now describe a study of S. aureus EssB, a 52-kDa bitopic membrane protein essential for secretion of the ESAT-6-family-proteins, the prototypic substrate of Type VII secretion. Full-length EssB was heterologously expressed in Escherichia coli, solubilised from the bacterial membrane, purified to homogeneity and shown to be dimeric. A C-terminal truncation, EssBC, and two soluble fragments termed EssB-N and EssB-C, predicted to occur on either side of the cytoplasmic membrane, have been successfully purified in recombinant form, characterised and together with the full-length protein used in crystallisation trials. EssB-N, the 25 kDa N-terminal cytoplasmic fragment, gave well-ordered crystals and we report the structure, determined by single-wavelength anomalous diffraction (SAD) targeting an SeMet derivative, refined to atomic (1.05 A) resolution. EssB-N is dimeric in solution but crystallises as a monomer and displays a fold composed of two globular domains separated by a cleft. The structure is related to that of Ser/Thr protein kinases and our study identifies that the type VII secretion system exploits and re-uses a stable modular entity and fold that has evolved to participate in protein-protein interactions in a similar fashion to the catalytically inert pseudokinases. Characterisation of Staphylococcus aureus EssB, an integral membrane component of the Type VII secretion system; atomic resolution crystal structure of the cytoplasmic segment.,Zoltner M, Fyfe PK, Palmer T, Hunter WN Biochem J. 2012 Oct 25. PMID:23098276[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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