6a0n: Difference between revisions
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The | ==The crystal structure of apo-Lpg2622== | ||
<StructureSection load='6a0n' size='340' side='right'caption='[[6a0n]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6a0n]] 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=6A0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A0N 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]] 2.1Å</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=6a0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a0n OCA], [https://pdbe.org/6a0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a0n RCSB], [https://www.ebi.ac.uk/pdbsum/6a0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a0n ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5ZS97_LEGPH Q5ZS97_LEGPH] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Legionella pneumophila type II secretion system can promote bacterial growth under a wide variety of conditions and mediates the secretion of more than 25 proteins, including the uncharacterized effector Lpg2622. Here, we determined the crystal structures of apo-Lpg2622 and Lpg2622 in complex with the cysteine protease inhibitor E64. Structural analysis suggests that Lpg2622 belongs to the C1 family peptidases. Interestingly, unlike the other structurally resolved papain-like cysteine proteases, the propeptide of Lpg2622 forms a novel super-secondary structural fold (hairpin-turn-helix) and can be categorized into a new group. In addition, the N-terminal beta-sheet of the Lpg2622 propeptide plays a regulatory role on enzymatic activity. This study enhances our understanding of the classification and regulatory mechanisms of the C1 family peptidases. | |||
Structural characterization of the hypothetical protein Lpg2622, a new member of the C1 family peptidases from Legionella pneumophila.,Gong X, Zhao X, Zhang W, Wang J, Chen X, Hameed MF, Zhang N, Ge H FEBS Lett. 2018 Aug;592(16):2798-2810. doi: 10.1002/1873-3468.13210. Epub 2018, Aug 20. PMID:30071124<ref>PMID:30071124</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6a0n" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]] | |||
[[Category: Ge H]] | |||
[[Category: Gong X]] | |||
Latest revision as of 05:01, 21 November 2024
The crystal structure of apo-Lpg2622
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