1ys4

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(New page: 200px<br /><applet load="1ys4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ys4, resolution 2.29&Aring;" /> '''Structure of Asparta...)
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[[Image:1ys4.jpg|left|200px]]<br /><applet load="1ys4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ys4, resolution 2.29&Aring;" />
 
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'''Structure of Aspartate-Semialdehyde Dehydrogenase from Methanococcus jannaschii'''<br />
 
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==Overview==
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==Structure of Aspartate-Semialdehyde Dehydrogenase from Methanococcus jannaschii==
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The structure of aspartate-beta-semialdehyde dehydrogenase (ASADH) from, Methanococcus jannaschii has been determined to 2.3 angstroms resolution, using multiwavelength anomalous diffraction (MAD) phasing of a, selenomethionine-substituted derivative to define a new branch in the, family of ASADHs. This new structure has a similar overall fold and domain, organization despite less than 10% conserved sequence identity with the, bacterial enzymes. However, the entire repertoire of functionally, important active site amino acid residues is conserved, suggesting an, identical catalytic mechanism but with lower catalytic efficiency. A new, coenzyme-binding conformation and dual NAD/NADP coenzyme specificity, further distinguish this archaeal branch from the bacterial ASADHs., Several structural differences are proposed to account for the, dramatically enhanced thermostability of this archaeal enzyme. Finally, the intersubunit communication channel connecting the active sites in the, bacterial enzyme dimer has been disrupted in the archaeal ASADHs by amino, acid changes that likely prevent the alternating sites reactivity, previously proposed for the bacterial ASADHs.
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<StructureSection load='1ys4' size='340' side='right'caption='[[1ys4]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ys4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YS4 FirstGlance]. <br>
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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]] 2.29&#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=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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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=1ys4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ys4 OCA], [https://pdbe.org/1ys4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ys4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ys4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ys4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DHAS_METJA DHAS_METJA] Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. To a lesser extent, is able to use NAD instead of NADP.<ref>PMID:16225889</ref>
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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/ys/1ys4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ys4 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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The structure of aspartate-beta-semialdehyde dehydrogenase (ASADH) from Methanococcus jannaschii has been determined to 2.3 angstroms resolution using multiwavelength anomalous diffraction (MAD) phasing of a selenomethionine-substituted derivative to define a new branch in the family of ASADHs. This new structure has a similar overall fold and domain organization despite less than 10% conserved sequence identity with the bacterial enzymes. However, the entire repertoire of functionally important active site amino acid residues is conserved, suggesting an identical catalytic mechanism but with lower catalytic efficiency. A new coenzyme-binding conformation and dual NAD/NADP coenzyme specificity further distinguish this archaeal branch from the bacterial ASADHs. Several structural differences are proposed to account for the dramatically enhanced thermostability of this archaeal enzyme. Finally, the intersubunit communication channel connecting the active sites in the bacterial enzyme dimer has been disrupted in the archaeal ASADHs by amino acid changes that likely prevent the alternating sites reactivity previously proposed for the bacterial ASADHs.
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==About this Structure==
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A new branch in the family: structure of aspartate-beta-semialdehyde dehydrogenase from Methanococcus jannaschii.,Faehnle CR, Ohren JF, Viola RE J Mol Biol. 2005 Nov 11;353(5):1055-68. Epub 2005 Sep 29. PMID:16225889<ref>PMID:16225889</ref>
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1YS4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with NAP and MLA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aspartate-semialdehyde_dehydrogenase Aspartate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.11 1.2.1.11] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YS4 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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A new branch in the family: structure of aspartate-beta-semialdehyde dehydrogenase from Methanococcus jannaschii., Faehnle CR, Ohren JF, Viola RE, J Mol Biol. 2005 Nov 11;353(5):1055-68. Epub 2005 Sep 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16225889 16225889]
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</div>
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[[Category: Aspartate-semialdehyde dehydrogenase]]
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<div class="pdbe-citations 1ys4" style="background-color:#fffaf0;"></div>
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[[Category: Methanocaldococcus jannaschii]]
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[[Category: Single protein]]
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[[Category: Faehnle, C.R.]]
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[[Category: Ohren, J.F.]]
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[[Category: Viola, R.E.]]
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[[Category: MLA]]
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[[Category: NAP]]
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[[Category: asadh]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:00:55 2007''
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==See Also==
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*[[Aspartate-semialdehyde dehydrogenase 3D structures|Aspartate-semialdehyde dehydrogenase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Methanocaldococcus jannaschii]]
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[[Category: Faehnle CR]]
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[[Category: Ohren JF]]
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[[Category: Viola RE]]

Current revision

Structure of Aspartate-Semialdehyde Dehydrogenase from Methanococcus jannaschii

PDB ID 1ys4

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