2x3b: Difference between revisions
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New page: '''Unreleased structure''' The entry 2x3b is ON HOLD until Paper Publication Authors: Bogdanovic, X., Palm, G.J., Singh, R.K., Hinrichs, W. Description: AsaP1 inactive mutant E294A, an... |
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==AsaP1 inactive mutant E294A, an extracellular toxic zinc metalloendopeptidase== | |||
<StructureSection load='2x3b' size='340' side='right'caption='[[2x3b]], [[Resolution|resolution]] 2.28Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2x3b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeromonas_salmonicida_subsp._achromogenes Aeromonas salmonicida subsp. achromogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X3B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X3B 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]] 2.28Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=2x3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x3b OCA], [https://pdbe.org/2x3b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x3b RCSB], [https://www.ebi.ac.uk/pdbsum/2x3b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x3b ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8GMV9_AERSA Q8GMV9_AERSA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Gram-negative bacterium Aeromonas salmonicida is a fish pathogen for various fish species worldwide. Aeromonas salmonicida subsp. achromogenes produces the extracellular, toxic zinc endopeptidase AsaP1. Crystal structure analyses at 2.0 A resolution of two proteolytically inactive AsaP1 variants show the polypeptide folding of the protease domain and the propeptide domain. These first crystal structure analyses of a precursor of a deuterolysin-like aspzincin protease provide insights into propeptide function, and specific substrate binding. A lysine side chain of the propeptide binds in the hydrophobic S1'-pocket interacting with three carboxylate side chains. An AsaP1 variant with a lysine to alanine exchange identifies the chaperone function of the propeptide. | |||
Structural evidence of intramolecular propeptide inhibition of the aspzincin metalloendopeptidase AsaP1.,Bogdanovic X, Palm GJ, Schwenteit J, Singh RK, Gudmundsdottir BK, Hinrichs W FEBS Lett. 2016 Aug 16. doi: 10.1002/1873-3468.12356. PMID:27528449<ref>PMID:27528449</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2x3b" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aeromonas salmonicida subsp. achromogenes]] | |||
[[Category: Large Structures]] | |||
[[Category: Bogdanovic X]] | |||
[[Category: Hinrichs W]] | |||
[[Category: Palm GJ]] | |||
[[Category: Singh RK]] | |||
