View source for 6fwy


==Thioester domain of the Enterococcus faecium TIE86 protein==
<StructureSection load='6fwy' size='340' side='right' caption='[[6fwy]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6fwy]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_19434 Atcc 19434]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FWY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FWY FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6fwv|6fwv]], [[6fx6|6fx6]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">B4W81_16995, BTA13_08335, DTPHA_1402599 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1352 ATCC 19434])</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=6fwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fwy OCA], [http://pdbe.org/6fwy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fwy RCSB], [http://www.ebi.ac.uk/pdbsum/6fwy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fwy ProSAT]</span></td></tr>
</table>
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6fwy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Atcc 19434]]
[[Category: Banfield, M J]]
[[Category: Miller, O K]]
[[Category: Schwarz-Linek, U]]
[[Category: Lpxtg-anchored]]
[[Category: Surface protein]]
[[Category: Thioester domain]]
[[Category: Tie protein]]
[[Category: Unknown function]]