6l6g: Difference between revisions

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'''Unreleased structure'''


The entry 6l6g is ON HOLD  until Oct 29 2021
==Crystal structure of SeMet_Lpg0189==
<StructureSection load='6l6g' size='340' side='right'caption='[[6l6g]], [[Resolution|resolution]] 1.98&Aring;' 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]] 1.98&#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=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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</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

6l6g is a 2 chain structure with sequence from Legionella pneumophila subsp. pneumophila str. Philadelphia 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.98Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q5ZZ22_LEGPH

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Chen X, Liu S, Jiang S, Zhang X, Zhang N, Ma J, Ge H. Crystal structure of a hypothetical T2SS effector Lpg0189 from Legionella pneumophila reveals a novel protein fold. Biochem Biophys Res Commun. 2019 Nov 6. pii: S0006-291X(19)32111-4. doi:, 10.1016/j.bbrc.2019.10.195. PMID:31706575 doi:http://dx.doi.org/10.1016/j.bbrc.2019.10.195

6l6g, resolution 1.98Å

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OCA