2x3a: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
(5 intermediate revisions by the same user not shown)
Line 1: Line 1:
==ASAP1 INACTIVE MUTANT E294Q, AN EXTRACELLULAR TOXIC ZINC METALLOENDOPEPTIDASE==
 
<StructureSection load='2x3a' size='340' side='right' caption='[[2x3a]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
==AsaP1 inactive mutant E294Q, an extracellular toxic zinc metalloendopeptidase==
<StructureSection load='2x3a' size='340' side='right'caption='[[2x3a]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2x3a]] is a 1 chain structure with sequence from [http://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=2X3A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X3A FirstGlance]. <br>
<table><tr><td colspan='2'>[[2x3a]] is a 1 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=2X3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X3A FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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]] 2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2x3b|2x3b]], [[2x3c|2x3c]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Deuterolysin Deuterolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.39 3.4.24.39] </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=2x3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x3a OCA], [https://pdbe.org/2x3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x3a RCSB], [https://www.ebi.ac.uk/pdbsum/2x3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x3a ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2x3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x3a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x3a RCSB], [http://www.ebi.ac.uk/pdbsum/2x3a PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8GMV9_AERSA Q8GMV9_AERSA]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Two mutants of the toxic extracellular zinc endopeptidase AsaP1 (AsaP1_E294Q and AsaP1_E294A) of Aeromonas salmonicida subsp. achromogenes were expressed in Escherichia coli and crystallized by the vapour-diffusion method. Crystals were obtained using several precipitants and different protein concentrations. Protein crystals were found in a monoclinic (C2) as well as an orthorhombic (P2(1)2(1)2(1)) space group. The crystals belonging to the monoclinic space group C2 had unit-cell parameters a = 103.4, b = 70.9, c = 54.9 A, beta = 109.3 degrees for AsaP1_E294A, and a = 98.5, b = 74.5, c = 54.7 A, beta = 112.4 degrees for AsaP1_E294Q. The unit-cell parameters of the orthorhombic crystal obtained for AsaP1_E294A were a = 57.9, b = 60.2, c = 183.6 A. The crystals of the two different mutants diffracted X-rays beyond 2.0 A resolution.
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.


Crystallization and preliminary X-ray diffraction studies of AsaP1_E294A and AsaP1_E294Q, two inactive mutants of the toxic zinc metallopeptidase AsaP1 from Aeromonas salmonicida subsp. achromogenes.,Bogdanovic X, Singh RK, Hentschke J, Gudmundsdottir BK, Hinrichs W Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jul 1;65(Pt, 7):695-7. Epub 2009 Jun 27. PMID:19574642<ref>PMID:19574642</ref>
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 2x3a" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
Line 21: Line 24:
</StructureSection>
</StructureSection>
[[Category: Aeromonas salmonicida subsp. achromogenes]]
[[Category: Aeromonas salmonicida subsp. achromogenes]]
[[Category: Deuterolysin]]
[[Category: Large Structures]]
[[Category: Bogdanovic, X.]]
[[Category: Bogdanovic X]]
[[Category: Hinrichs, W.]]
[[Category: Hinrichs W]]
[[Category: Palm, G J.]]
[[Category: Palm GJ]]
[[Category: Singh, R K.]]
[[Category: Singh RK]]
[[Category: Hydrolase]]
Retrieved from "https://proteopedia.org/2x3a"