3iwj

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{{Seed}}
 
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[[Image:3iwj.jpg|left|200px]]
 
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==Crystal structure of aminoaldehyde dehydrogenase 2 from Pisum sativum (PsAMADH2)==
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The line below this paragraph, containing "STRUCTURE_3iwj", creates the "Structure Box" on the page.
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<StructureSection load='3iwj' size='340' side='right'caption='[[3iwj]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3iwj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IWJ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
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<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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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{{STRUCTURE_3iwj| PDB=3iwj | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3iwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iwj OCA], [https://pdbe.org/3iwj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iwj RCSB], [https://www.ebi.ac.uk/pdbsum/3iwj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iwj ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AADH2_PEA AADH2_PEA] Dehydrogenase that catalyzes the oxidation of several aminoaldehydes (PubMed:20026072). Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 3-aminopropanal to beta-alanine (Ref.1, PubMed:20026072, PubMed:21740525). Catalyzes the oxidation of 4-aminobutanal to 4-aminobutanoate (PubMed:20026072, PubMed:21740525). Catalyzes the oxidation of 4-guanidinobutanal to 4-guanidinobutanoate (PubMed:20026072).<ref>PMID:20026072</ref> <ref>PMID:21740525</ref> [UniProtKB:P20000]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iw/3iwj_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3iwj ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Aminoaldehyde dehydrogenases (AMADHs, EC 1.2.1.19) belong to the large aldehyde dehydrogenase (ALDH) superfamily, namely, the ALDH9 family. They oxidize polyamine-derived omega-aminoaldehydes to the corresponding omega-amino acids. Here, we report the first X-ray structures of plant AMADHs: two isoenzymes, PsAMADH1 and PsAMADH2, from Pisum sativum in complex with beta-nicotinamide adenine dinucleotide (NAD(+)) at 2.4 and 2.15 A resolution, respectively. Both recombinant proteins are dimeric and, similarly to other ALDHs, each monomer is composed of an oligomerization domain, a coenzyme binding domain and a catalytic domain. Each subunit binds NAD(+) as a coenzyme, contains a solvent-accessible C-terminal peroxisomal targeting signal (type 1) and a cation bound in the cavity close to the NAD(+) binding site. While the NAD(+) binding mode is classical for PsAMADH2, that for PsAMADH1 is unusual among ALDHs. A glycerol molecule occupies the substrate binding site and mimics a bound substrate. Structural analysis and substrate specificity study of both isoenzymes in combination with data published previously on other ALDH9 family members show that the established categorization of such enzymes into distinct groups based on substrate specificity is no more appropriate, because many of them seem capable of oxidizing a large spectrum of aminoaldehyde substrates. PsAMADH1 and PsAMADH2 can oxidize N,N,N-trimethyl-4-aminobutyraldehyde into gamma-butyrobetaine, which is the carnitine precursor in animal cells. This activity highly suggests that in addition to their contribution to the formation of compatible osmolytes such as glycine betaine, beta-alanine betaine and gamma-aminobutyric acid, AMADHs might participate in carnitine biosynthesis in plants.
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===Crystal structure of aminoaldehyde dehydrogenase 2 from Pisum sativum (PsAMADH2)===
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Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes.,Tylichova M, Kopecny D, Morera S, Briozzo P, Lenobel R, Snegaroff J, Sebela M J Mol Biol. 2010 Mar 5;396(4):870-82. Epub 2009 Dec 21. PMID:20026072<ref>PMID:20026072</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_20026072}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3iwj" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20026072 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20026072}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3IWJ is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IWJ OCA].
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==Reference==
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<ref group="xtra">PMID:20026072</ref><references group="xtra"/>
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[[Category: Aminobutyraldehyde dehydrogenase]]
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[[Category: Pisum sativum]]
[[Category: Pisum sativum]]
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[[Category: Briozzo, P.]]
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[[Category: Briozzo P]]
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[[Category: Kopecny, D.]]
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[[Category: Kopecny D]]
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[[Category: Morera, S.]]
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[[Category: Morera S]]
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[[Category: Aminoaldehyde dehydrogenase]]
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[[Category: Betaine aldehyde dehydrogenase]]
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[[Category: Dimer]]
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[[Category: Nad]]
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[[Category: Oxidoreductase]]
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[[Category: Rossmann fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 20 15:51:33 2010''
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Current revision

Crystal structure of aminoaldehyde dehydrogenase 2 from Pisum sativum (PsAMADH2)

PDB ID 3iwj

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