6a0n

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'''Unreleased structure'''
 
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The entry 6a0n is ON HOLD until Paper Publication
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==The crystal structure of apo-Lpg2622==
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<StructureSection load='6a0n' size='340' side='right'caption='[[6a0n]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q5ZS97_LEGPH Q5ZS97_LEGPH]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Gong, X., Ge, H.
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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>
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Description: The crystal structure of apo-Lpg2622
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Ge, H]]
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<div class="pdbe-citations 6a0n" style="background-color:#fffaf0;"></div>
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[[Category: Gong, X]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]]
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[[Category: Ge H]]
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[[Category: Gong X]]

Current revision

The crystal structure of apo-Lpg2622

PDB ID 6a0n

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