2ynq: Difference between revisions
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The | ==Crystal Structure of Geobacillus thermodenitrificans EssB extracellular fragment== | ||
<StructureSection load='2ynq' size='340' side='right'caption='[[2ynq]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2ynq]] is a 4 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=2YNQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YNQ 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]] 2.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=2ynq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ynq OCA], [https://pdbe.org/2ynq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ynq RCSB], [https://www.ebi.ac.uk/pdbsum/2ynq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ynq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A4IKE6_GEOTN A4IKE6_GEOTN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The membrane-bound EssB is an integral and essential component of the bacterial type VII secretion system that can contribute to pathogenicity. The architecture of Geobacillus thermodenitrificans EssB has been investigated by combining crystallographic and EPR spectroscopic methods. The protein forms a dimer that straddles the cytoplasmic membrane. A helical fold is observed for the C-terminal segment, which is positioned on the exterior of the membrane. This segment contributes most to dimer formation. The N-terminal segment displays a structure related to the pseudokinase fold and may contribute to function by recognizing substrates or secretion system partners. The remaining part of EssB may serve as an anchor point for the secretion apparatus, which is embedded in the cytoplasmic membrane with the C-terminal domain protruding out to interact with partner proteins or components of peptidoglycan. | |||
The architecture of EssB, an integral membrane component of the type VII secretion system.,Zoltner M, Norman DG, Fyfe PK, El Mkami H, Palmer T, Hunter WN Structure. 2013 Apr 2;21(4):595-603. doi: 10.1016/j.str.2013.02.007. Epub 2013, Mar 14. PMID:23499020<ref>PMID:23499020</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2ynq" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Geobacillus thermodenitrificans NG80-2]] | |||
[[Category: Large Structures]] | |||
[[Category: Fyfe PK]] | |||
[[Category: Hunter WN]] | |||
[[Category: Zoltner M]] | |||
Latest revision as of 17:06, 1 February 2024
Crystal Structure of Geobacillus thermodenitrificans EssB extracellular fragmentCrystal Structure of Geobacillus thermodenitrificans EssB extracellular fragment
Structural highlights
FunctionPublication Abstract from PubMedThe membrane-bound EssB is an integral and essential component of the bacterial type VII secretion system that can contribute to pathogenicity. The architecture of Geobacillus thermodenitrificans EssB has been investigated by combining crystallographic and EPR spectroscopic methods. The protein forms a dimer that straddles the cytoplasmic membrane. A helical fold is observed for the C-terminal segment, which is positioned on the exterior of the membrane. This segment contributes most to dimer formation. The N-terminal segment displays a structure related to the pseudokinase fold and may contribute to function by recognizing substrates or secretion system partners. The remaining part of EssB may serve as an anchor point for the secretion apparatus, which is embedded in the cytoplasmic membrane with the C-terminal domain protruding out to interact with partner proteins or components of peptidoglycan. The architecture of EssB, an integral membrane component of the type VII secretion system.,Zoltner M, Norman DG, Fyfe PK, El Mkami H, Palmer T, Hunter WN Structure. 2013 Apr 2;21(4):595-603. doi: 10.1016/j.str.2013.02.007. Epub 2013, Mar 14. PMID:23499020[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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