6fwv: Difference between revisions
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The | ==The Bacillus anthracis TIE protein== | ||
<StructureSection load='6fwv' size='340' side='right'caption='[[6fwv]], [[Resolution|resolution]] 2.58Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6fwv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FWV 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]] 2.58Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6fwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fwv OCA], [https://pdbe.org/6fwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fwv RCSB], [https://www.ebi.ac.uk/pdbsum/6fwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fwv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A6L8P957_BACAN A0A6L8P957_BACAN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
An increasing number of surface-associated proteins identified in Gram-positive bacteria are characterized by intramolecular cross-links in structurally conserved thioester, isopeptide, and ester domains (TIE proteins). Two classes of thioester domains (TEDs) have been predicted based on sequence with, to date, only representatives of class I structurally characterized. Here, we present crystal structures of three class II TEDs from Bacillus anthracis, vancomycin-resistant Staphylococcus aureus, and vancomycin-resistant Enterococcus faecium. These proteins are structurally distinct from class I TEDs due to a beta-sandwich domain that is inserted into the conserved TED fold to form a slipknot structure. Further, the B. anthracis TED domain is presented in the context of a full-length sortase-anchored protein structure (BaTIE). This provides insight into the three-dimensional arrangement of TIE proteins, which emerge as very abundant putative adhesins of Gram-positive bacteria. This article is protected by copyright. All rights reserved. | |||
A new structural class of bacterial thioester domains reveals a slipknot topology.,Miller OK, Banfield MJ, Schwarz-Linek U Protein Sci. 2018 Jul 27. doi: 10.1002/pro.3478. PMID:30052296<ref>PMID:30052296</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6fwv" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Adhesin 3D structures|Adhesin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus anthracis]] | |||
[[Category: Large Structures]] | |||
[[Category: Banfield MJ]] | |||
[[Category: Miller OK]] | |||
[[Category: Schwarz-Linek U]] | |||
Latest revision as of 08:42, 5 June 2024
The Bacillus anthracis TIE proteinThe Bacillus anthracis TIE protein
Structural highlights
FunctionPublication Abstract from PubMedAn increasing number of surface-associated proteins identified in Gram-positive bacteria are characterized by intramolecular cross-links in structurally conserved thioester, isopeptide, and ester domains (TIE proteins). Two classes of thioester domains (TEDs) have been predicted based on sequence with, to date, only representatives of class I structurally characterized. Here, we present crystal structures of three class II TEDs from Bacillus anthracis, vancomycin-resistant Staphylococcus aureus, and vancomycin-resistant Enterococcus faecium. These proteins are structurally distinct from class I TEDs due to a beta-sandwich domain that is inserted into the conserved TED fold to form a slipknot structure. Further, the B. anthracis TED domain is presented in the context of a full-length sortase-anchored protein structure (BaTIE). This provides insight into the three-dimensional arrangement of TIE proteins, which emerge as very abundant putative adhesins of Gram-positive bacteria. This article is protected by copyright. All rights reserved. A new structural class of bacterial thioester domains reveals a slipknot topology.,Miller OK, Banfield MJ, Schwarz-Linek U Protein Sci. 2018 Jul 27. doi: 10.1002/pro.3478. PMID:30052296[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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