6l6g: Difference between revisions
No edit summary |
No edit summary |
||
(One intermediate revision by the same user not shown) | |||
Line 1: | Line 1: | ||
==Crystal structure of SeMet_Lpg0189== | |||
<StructureSection load='6l6g' size='340' side='right'caption='[[6l6g]], [[Resolution|resolution]] 1.98Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6l6g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_str._Philadelphia_1 Legionella pneumophila subsp. pneumophila str. Philadelphia 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L6G 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]] 1.98Å</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=MSE:SELENOMETHIONINE'>MSE</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=6l6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l6g OCA], [https://pdbe.org/6l6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l6g RCSB], [https://www.ebi.ac.uk/pdbsum/6l6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l6g ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5ZZ22_LEGPH Q5ZZ22_LEGPH] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Lpg0189 is a type II secretion system-dependent extracellular protein with unknown function from Legionella pneumophila. Herein, we determined the crystal structure of Lpg0189 at 1.98A resolution by using single-wavelength anomalous diffraction (SAD). Lpg0189 folds into a novel chair-shaped architecture, with two sheets roughly perpendicular to each other. Bioinformatics analysis suggests Lpg0189 and its homologues are unique to Legionellales and evolved divergently. The interlinking structural and bioinformatics studies provide a better understanding of this hypothetical protein. | |||
Crystal structure of a hypothetical T2SS effector Lpg0189 from Legionella pneumophila reveals a novel protein fold.,Chen X, Liu S, Jiang S, Zhang X, Zhang N, Ma J, Ge H Biochem Biophys Res Commun. 2019 Nov 6. pii: S0006-291X(19)32111-4. doi:, 10.1016/j.bbrc.2019.10.195. PMID:31706575<ref>PMID:31706575</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6l6g" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]] | |||
[[Category: Chen X]] | |||
[[Category: Ge H]] |
Latest revision as of 14:10, 30 October 2024
Crystal structure of SeMet_Lpg0189Crystal structure of SeMet_Lpg0189
Structural highlights
FunctionPublication Abstract from PubMedLpg0189 is a type II secretion system-dependent extracellular protein with unknown function from Legionella pneumophila. Herein, we determined the crystal structure of Lpg0189 at 1.98A resolution by using single-wavelength anomalous diffraction (SAD). Lpg0189 folds into a novel chair-shaped architecture, with two sheets roughly perpendicular to each other. Bioinformatics analysis suggests Lpg0189 and its homologues are unique to Legionellales and evolved divergently. The interlinking structural and bioinformatics studies provide a better understanding of this hypothetical protein. Crystal structure of a hypothetical T2SS effector Lpg0189 from Legionella pneumophila reveals a novel protein fold.,Chen X, Liu S, Jiang S, Zhang X, Zhang N, Ma J, Ge H Biochem Biophys Res Commun. 2019 Nov 6. pii: S0006-291X(19)32111-4. doi:, 10.1016/j.bbrc.2019.10.195. PMID:31706575[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
|