View source for 3obb

==Crystal structure of a possible 3-hydroxyisobutyrate Dehydrogenase from pseudomonas aeruginosa pao1==
<StructureSection load='3obb' size='340' side='right' caption='[[3obb]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3obb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. This structure supersedes the now removed PDB entries  and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2h78 2h78]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OBB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OBB FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene><br>
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA0743 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Serine_3-dehydrogenase Serine 3-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.276 1.1.1.276] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3obb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3obb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3obb RCSB], [http://www.ebi.ac.uk/pdbsum/3obb PDBsum]</span></td></tr>
<table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ob/3obb_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The beta-hydroxyacid dehydrogenases form a large family of ubiquitous enzymes that catalyze oxidation of various beta-hydroxy acid substrates to corresponding semialdehydes. Several known enzymes include beta-hydroxyisobutyrate dehydrogenase, 6-phosphogluconate dehydrogenase, 2-(hydroxymethyl)glutarate dehydrogenase, and phenylserine dehydrogenase, but the vast majority of beta-hydroxyacid dehydrogenases remain uncharacterized. Here, we demonstrate that the predicted beta-hydroxyisobutyrate dehydrogenase PA0743 from Pseudomonas aeruginosa catalyzes an NAD(+)-dependent oxidation of l-serine and methyl-l-serine but exhibits low activity against beta-hydroxyisobutyrate. Two crystal structures of PA0743 were solved at 2.2-2.3-A resolution and revealed an N-terminal Rossmann fold domain connected by a long alpha-helix to the C-terminal all-alpha domain. The PA0743 apostructure showed the presence of additional density modeled as HEPES bound in the interdomain cleft close to the predicted catalytic Lys-171, revealing the molecular details of the PA0743 substrate-binding site. The structure of the PA0743-NAD(+) complex demonstrated that the opposite side of the enzyme active site accommodates the cofactor, which is also bound near Lys-171. Site-directed mutagenesis of PA0743 emphasized the critical role of four amino acid residues in catalysis including the primary catalytic residue Lys-171. Our results provide further insight into the molecular mechanisms of substrate selectivity and activity of beta-hydroxyacid dehydrogenases.

Biochemical and Structural Studies of Uncharacterized Protein PA0743 from Pseudomonas aeruginosa Revealed NAD+-dependent L-Serine Dehydrogenase.,Tchigvintsev A, Singer A, Brown G, Flick R, Evdokimova E, Tan K, Gonzalez CF, Savchenko A, Yakunin AF J Biol Chem. 2012 Jan 13;287(3):1874-83. Epub 2011 Nov 28. PMID:22128181<ref>PMID:22128181</ref>

From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Pseudomonas aeruginosa]]
[[Category: Serine 3-dehydrogenase]]
[[Category: Edwards, A M.]]
[[Category: Evdokimova, E.]]
[[Category: Joachimiak, A.]]
[[Category: Kudritska, M.]]
[[Category: MCSG, Midwest Center for Structural Genomics.]]
[[Category: Savchenko, A.]]
[[Category: Singer, A U.]]
[[Category: Tan, K.]]
[[Category: Yakunin, A F.]]
[[Category: Alpha-beta]]
[[Category: Mcsg]]
[[Category: Midwest center for structural genomic]]
[[Category: Oxidoreductase]]
[[Category: Protein structure initiative]]
[[Category: Psi-2]]
[[Category: Serine dehydrogenase]]
[[Category: Structural genomic]]