5l44: Difference between revisions
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<StructureSection load='5l44' size='340' side='right'caption='[[5l44]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='5l44' size='340' side='right'caption='[[5l44]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5l44]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5l44]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Astrosporangium_hypotensionis_K-26 Astrosporangium hypotensionis K-26]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L44 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K26:N-ACETYL-L-ILE-L-TYR-(R)-1-AMINO-2-(4-HYDROXYPHENYL)ETHYLPHOSPHONIC+ACID'>K26</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.75Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K26:N-ACETYL-L-ILE-L-TYR-(R)-1-AMINO-2-(4-HYDROXYPHENYL)ETHYLPHOSPHONIC+ACID'>K26</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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=5l44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l44 OCA], [https://pdbe.org/5l44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l44 RCSB], [https://www.ebi.ac.uk/pdbsum/5l44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l44 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A1L1QK30_9ACTN A0A1L1QK30_9ACTN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 23: | Line 26: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Astrosporangium hypotensionis | [[Category: Astrosporangium hypotensionis K-26]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Acharya | [[Category: Acharya KR]] | ||
[[Category: Bachmann | [[Category: Bachmann BO]] | ||
[[Category: Kramer | [[Category: Kramer GJ]] | ||
[[Category: Masuyer | [[Category: Masuyer G]] | ||
Latest revision as of 19:06, 4 October 2023
Structure of K-26-DCP in complex with the K-26 tripeptideStructure of K-26-DCP in complex with the K-26 tripeptide
Structural highlights
FunctionPublication Abstract from PubMedSeveral soil-derived actinobacteria produce secondary metabolites that are proven specific and potent inhibitors of the human angiotensin-I converting enzyme (ACE), a key target for the modulation of hypertension through its role in the renin-angiotensin-aldosterone system. K-26-DCP is a zinc dipeptidyl carboxypeptidase produced by Astrosporangium hypotensionis, and an ancestral homologue of ACE. Here we report the high resolution crystal structures of K-26-DCP and of its complex with the natural microbial tripeptide product K-26. The experimental results provide the structural basis for better understanding the specificity of K-26 for human ACE over bacterial DCPs. This article is protected by copyright. All rights reserved. Crystal structure of a peptidyl-dipeptidase K-26-DCP from Actinomycete in complex with its natural inhibitor.,Masuyer G, Cozier GE, Kramer GJ, Bachmann BO, Acharya KR FEBS J. 2016 Oct 18. doi: 10.1111/febs.13928. PMID:27754586[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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