6a0q: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

The ~~entry~~ 6a0q is ~~ON HOLD until Paper~~ Publication

==The crystal structure of Lpg2622_E64 complex==

== 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>

== 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.

~~Authors: Xiaojian~~, G., ~~Honghua~~, G.

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>

~~Description~~: ~~The crystal structure of Lpg2622_E64 complex~~

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

[[Category: ~~Unreleased Structures~~]]

</div>

[[Category: ~~Honghua~~, G]]

[[Category: ~~Xiaojian, G~~]]

== References ==

__TOC__

</StructureSection>

[[Category: Ge, H]]

[[Category: Gong, X]]

[[Category: Cysteine protease]]

[[Category: Hydrolase]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6a0q is ON HOLD  until Paper Publication
+==The crystal structure of Lpg2622_E64 complex==
+<StructureSection load='6a0q' size='340' side='right' caption='[[6a0q]], [[Resolution|resolution]] 2.20&Aring;' 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.
-Authors: Xiaojian, G., Honghua, G.
+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>
-Description: The crystal structure of Lpg2622_E64 complex
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Honghua, G]]
+<div class="pdbe-citations 6a0q" style="background-color:#fffaf0;"></div>
-[[Category: Xiaojian, G]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Ge, H]]
+[[Category: Gong, X]]
+[[Category: Cysteine protease]]
+[[Category: Hydrolase]]