2x3c

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:17, 9 August 2023) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
-
==ASAP1 INACTIVE MUTANT E294Q, AN EXTRACELLULAR TOXIC ZINC METALLOENDOPEPTIDASE==
+
==AsaP1 inactive mutant E294Q, an extracellular toxic zinc metalloendopeptidase==
-
<StructureSection load='2x3c' size='340' side='right' caption='[[2x3c]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
+
<StructureSection load='2x3c' size='340' side='right'caption='[[2x3c]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2x3c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"necromonas_achromogenes"_smith_1963 "necromonas achromogenes" smith 1963]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X3C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X3C FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2x3c]] 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=2X3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X3C FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.99&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2x3b|2x3b]], [[2x3a|2x3a]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=2x3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x3c OCA], [https://pdbe.org/2x3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x3c RCSB], [https://www.ebi.ac.uk/pdbsum/2x3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x3c 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=2x3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x3c OCA], [http://pdbe.org/2x3c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x3c RCSB], [http://www.ebi.ac.uk/pdbsum/2x3c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x3c ProSAT]</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>
Line 22: Line 23:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Necromonas achromogenes smith 1963]]
+
[[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]]
+

Current revision

AsaP1 inactive mutant E294Q, an extracellular toxic zinc metalloendopeptidase

PDB ID 2x3c

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2x3c"
Personal tools