7v9n: Difference between revisions

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<StructureSection load='7v9n' size='340' side='right'caption='[[7v9n]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='7v9n' size='340' side='right'caption='[[7v9n]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7v9n]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V9N FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V9N FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=7v9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v9n OCA], [https://pdbe.org/7v9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v9n RCSB], [https://www.ebi.ac.uk/pdbsum/7v9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v9n ProSAT]</span></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=7v9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v9n OCA], [https://pdbe.org/7v9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v9n RCSB], [https://www.ebi.ac.uk/pdbsum/7v9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v9n ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lanthipeptides are an important group of natural products with diverse biological functions, and their biosynthesis requires the removal of N-terminal leader peptides (LPs) by designated proteases. LanPM1 enzymes, a subgroup of M1 zinc-metallopeptidases, have been recently identified as bifunctional proteases with both endo- and aminopeptidase activities to remove LPs of class III and class IV lanthipeptides. Herein, we report the biochemical and structural characterization of EryP as the LanPM1 enzyme from the biosynthesis of class III lanthipeptide erythreapeptin. We determined X-ray crystal structures of EryP in three conformational states, the open, intermediate and closed states, and identified a unique interdomain Ca(2+) binding site as a regulatory element that modulates its domain dynamics and proteolytic activity. Inspired by this regulatory Ca(2+) binding, we developed a strategy to engineer LanPM1 enzymes for enhanced catalytic activities by strengthening interdomain associations and driving the conformational equilibrium toward their closed forms.


Conformational remodeling enhances activity of lanthipeptide zinc-metallopeptidases.,Zhao C, Sheng W, Wang Y, Zheng J, Xie X, Liang Y, Wei W, Bao R, Wang H Nat Chem Biol. 2022 May 5. pii: 10.1038/s41589-022-01018-2. doi:, 10.1038/s41589-022-01018-2. PMID:35513512<ref>PMID:35513512</ref>
==See Also==
 
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7v9n" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Membrane alanyl aminopeptidase]]
[[Category: Bao R]]
[[Category: Bao, R]]
[[Category: Zhao C]]
[[Category: Zhao, C]]
[[Category: Zhao NL]]
[[Category: Zhao, N L]]
[[Category: Alanine aminopeptidase]]
[[Category: Aminopeptidase]]
[[Category: Cytosolic protein]]
[[Category: Hydrolase]]

Latest revision as of 19:42, 29 May 2024

Crystal structure of the lanthipeptide zinc-metallopeptidase EryP from saccharopolyspora erythraea in closed state

7v9n, resolution 1.90Å

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