2qqc: Difference between revisions
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==E109Q mutant of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannashii== | ==E109Q mutant of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannashii== | ||
<StructureSection load='2qqc' size='340' side='right' caption='[[2qqc]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2qqc' size='340' side='right'caption='[[2qqc]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2qqc]] is a 12 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2qqc]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QQC FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AG2:AGMATINE'>AG2</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AG2:AGMATINE'>AG2</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qqd|2qqd]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2qqd|2qqd]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pdaD ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pdaD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Arginine_decarboxylase Arginine decarboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.19 4.1.1.19] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qqc OCA], [https://pdbe.org/2qqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qqc RCSB], [https://www.ebi.ac.uk/pdbsum/2qqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qqc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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[[Category: Arginine decarboxylase]] | [[Category: Arginine decarboxylase]] | ||
[[Category: Atcc 43067]] | [[Category: Atcc 43067]] | ||
[[Category: Large Structures]] | |||
[[Category: Ealick, S E]] | [[Category: Ealick, S E]] | ||
[[Category: Soriano, E S]] | [[Category: Soriano, E S]] | ||
Revision as of 11:29, 25 June 2021
E109Q mutant of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannashiiE109Q mutant of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannashii
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPyruvoyl-dependent arginine decarboxylase (PvlArgDC) catalyzes the first step of the polyamine-biosynthetic pathway in plants and some archaebacteria. The pyruvoyl group of PvlArgDC is generated by an internal autoserinolysis reaction at an absolutely conserved serine residue in the proenzyme, resulting in two polypeptide chains. Based on the native structure of PvlArgDC from Methanococcus jannaschii, the conserved residues Asn47 and Glu109 were proposed to be involved in the decarboxylation and autoprocessing reactions. N47A and E109Q mutant proteins were prepared and the three-dimensional structure of each protein was determined at 2.0 A resolution. The N47A and E109Q mutant proteins showed reduced decarboxylation activity compared with the wild-type PvlArgDC. These residues may also be important for the autoprocessing reaction, which utilizes a mechanism similar to that of the decarboxylation reaction. Structures of the N47A and E109Q mutant proteins of pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii.,Soriano EV, McCloskey DE, Kinsland C, Pegg AE, Ealick SE Acta Crystallogr D Biol Crystallogr. 2008 Apr;64(Pt 4):377-82. Epub 2008, Mar 19. PMID:18391404[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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