6aeo: Difference between revisions

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<StructureSection load='6aeo' size='340' side='right'caption='[[6aeo]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='6aeo' size='340' side='right'caption='[[6aeo]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6aeo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AEO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AEO FirstGlance]. <br>
<table><tr><td colspan='2'>[[6aeo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7] and [https://en.wikipedia.org/wiki/Serratia_surfactantfaciens Serratia surfactantfaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AEO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AEO 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></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=6aeo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aeo OCA], [http://pdbe.org/6aeo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aeo RCSB], [http://www.ebi.ac.uk/pdbsum/6aeo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aeo ProSAT]</span></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></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=6aeo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aeo OCA], [https://pdbe.org/6aeo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6aeo RCSB], [https://www.ebi.ac.uk/pdbsum/6aeo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6aeo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MALE_ECO57 MALE_ECO57]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides (By similarity).
[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Type VI secretion system (T6SS), as a macromolecular system, is commonly found in Gram-negative bacteria and responsible for exporting effectors. T6SS consists of 13 core proteins. TssL is a component of the membrane complex and plays a pivotal role in T6SS. Here, we report the crystal structure of the C-terminal periplasmic domain of TssL (TssLCter) from Serratia marcescens FS14. The TssLCter (310-503) contain a five-stranded anti-parallel beta-sheet flanked by five alpha-helices and a short N-terminal helix. Structural comparisons revealed that it belongs to the OmpA-like family with a remarked difference in the conformation of the loop3-5. In OmpA-like family, the corresponding loop is located close to loop2-3, forming a cavity with a small opening together with the longest alpha5, whereas in TssLCter, loop3-5 flipped away from this cavity region. In addition, significant differences in the peptidoglycan (PG) binding site suggest that big conformational change must take place to accomplish the PG binding for TssLCter. Furthermore, a long flexible loop between helices alpha1 and alpha2 is unique in TssL. TssL would have a big conformational change during the delivery of the Hcp needle and effectors. So we speculate that the long flexible endows TssL the adaptation of its evolutionary new function.


Crystal structure of the periplasmic domain of TssL, a key membrane component of Type VI secretion system.,Wang X, Sun B, Xu M, Qiu S, Xu D, Ran T, He J, Wang W Int J Biol Macromol. 2018 Dec;120(Pt B):1474-1479. doi:, 10.1016/j.ijbiomac.2018.09.166. Epub 2018 Sep 26. PMID:30266644<ref>PMID:30266644</ref>
==See Also==
 
*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6aeo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli O157:H7]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ran, T T]]
[[Category: Serratia surfactantfaciens]]
[[Category: Wang, W W]]
[[Category: Ran TT]]
[[Category: Wang, X B]]
[[Category: Wang WW]]
[[Category: Xu, D Q]]
[[Category: Wang XB]]
[[Category: Protein transport]]
[[Category: Xu DQ]]
[[Category: Structural protein]]

Latest revision as of 10:31, 27 March 2024

TssL periplasmic domain

6aeo, resolution 2.30Å

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