4ann: Difference between revisions
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==Crystal Structure Staphylococcus aureus ESSB cytoplasmic fragment== | ==Crystal Structure Staphylococcus aureus ESSB cytoplasmic fragment== | ||
<StructureSection load='4ann' size='340' side='right' caption='[[4ann]], [[Resolution|resolution]] 1.05Å' scene=''> | <StructureSection load='4ann' size='340' side='right' caption='[[4ann]], [[Resolution|resolution]] 1.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ann]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4ann]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staa8 Staa8]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ANN FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ano|4ano]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ano|4ano]]</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=4ann FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ann OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ann RCSB], [http://www.ebi.ac.uk/pdbsum/4ann PDBsum]</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=4ann FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ann OCA], [http://pdbe.org/4ann PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ann RCSB], [http://www.ebi.ac.uk/pdbsum/4ann PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ann ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4ann" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Staa8]] | ||
[[Category: Fyfe, P K]] | [[Category: Fyfe, P K]] | ||
[[Category: Hunter, W N]] | [[Category: Hunter, W N]] | ||
Revision as of 11:48, 11 August 2016
Crystal Structure Staphylococcus aureus ESSB cytoplasmic fragmentCrystal Structure Staphylococcus aureus ESSB cytoplasmic fragment
Structural highlights
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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