View source for 5gne


==Crystal structure of LapB from Legionella pneumophila==
<StructureSection load='5gne' size='340' side='right'caption='[[5gne]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5gne]] 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=5GNE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GNE 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5gne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gne OCA], [https://pdbe.org/5gne PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gne RCSB], [https://www.ebi.ac.uk/pdbsum/5gne PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gne ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5ZZH8_LEGPH Q5ZZH8_LEGPH] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Aminopeptidases are a group of exopeptidases that catalyze the removal of a wide range of N-terminal amino acid residues from peptides and proteins. They have many important commercial applications in the food industry. We determined the crystal structure of an aminopeptidase LapB from Legionella pneumophila. The overall structure reveals that the N-terminal protease-associated (PA) domain presents a new fold and shields the active site cavity of the conserved C-terminal peptidase domain. The steady-state kinetic analysis of LapB and the PA domain deletion mutant indicate that the PA domain inhibited enzyme activity of the peptidase domain. Interestingly, the activity of LapB was largely increased by various organic solvents such as ethanol, propanol, and methanol at the concentration of 60% (v/v). CD analysis provided evidence that organic solvents induce the PA domain conformational changes that eliminate the inhibition role. The unique properties indicate the application potential of LapB in the food processing industry.

Crystal Structure and Biochemical Characterization of an Aminopeptidase LapB from Legionella pneumophila.,Zhang N, Yin S, Zhang W, Gong X, Zhang N, Fang K, Ge H J Agric Food Chem. 2017 Aug 17. doi: 10.1021/acs.jafc.7b02849. PMID:28776986<ref>PMID:28776986</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5gne" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]]
[[Category: Ge H]]
[[Category: Zhang N]]