6a0q: Difference between revisions
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The | ==The crystal structure of Lpg2622_E64 complex== | ||
<StructureSection load='6a0q' size='340' side='right' caption='[[6a0q]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6a0q]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A0Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A0Q FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene></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=6a0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a0q OCA], [http://pdbe.org/6a0q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a0q RCSB], [http://www.ebi.ac.uk/pdbsum/6a0q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a0q ProSAT]</span></td></tr> | |||
</table> | |||
<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 6a0q" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ge, H]] | |||
[[Category: Gong, X]] | |||
[[Category: Cysteine protease]] | |||
[[Category: Hydrolase]] | |||
Revision as of 07:29, 12 September 2018
The crystal structure of Lpg2622_E64 complex
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