6fwy: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6fwy is ON HOLD  until Paper Publication
+==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 [https://en.wikipedia.org/wiki/Enterococcus_faecium Enterococcus faecium]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6FWY 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]] 2.14&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=6fwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fwy OCA], [https://pdbe.org/6fwy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fwy RCSB], [https://www.ebi.ac.uk/pdbsum/6fwy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fwy ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A1A7T0E1_ENTFC A0A1A7T0E1_ENTFC]
+<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.
-Authors: Miller, O.K., Banfield, M.J., Schwarz-Linek, U.
+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>
-Description: Thioester domain of the Enterococcus faecium TIE86 protein
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Banfield, M.J]]
+<div class="pdbe-citations 6fwy" style="background-color:#fffaf0;"></div>
-[[Category: Schwarz-Linek, U]]
+== References ==
-[[Category: Miller, O.K]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Enterococcus faecium]]
+[[Category: Large Structures]]
+[[Category: Banfield MJ]]
+[[Category: Miller OK]]
+[[Category: Schwarz-Linek U]]