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[[Image:3obb.png|left|200px]]
==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.


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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>
The line below this paragraph, containing "STRUCTURE_3obb", creates the "Structure Box" on the page.
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{{STRUCTURE_3obb|  PDB=3obb  |  SCENE=  }}


===Crystal structure of a possible 3-hydroxyisobutyrate Dehydrogenase from pseudomonas aeruginosa pao1===
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
</div>
 
== References ==
<!--
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The line below this paragraph, {{ABSTRACT_PUBMED_22128181}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 22128181 is the PubMed ID number.
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{{ABSTRACT_PUBMED_22128181}}
 
==About this Structure==
[[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].
 
==Reference==
<ref group="xtra">PMID:022128181</ref><references group="xtra"/>
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Serine 3-dehydrogenase]]
[[Category: Serine 3-dehydrogenase]]

Revision as of 13:43, 28 May 2014

Crystal structure of a possible 3-hydroxyisobutyrate Dehydrogenase from pseudomonas aeruginosa pao1Crystal structure of a possible 3-hydroxyisobutyrate Dehydrogenase from pseudomonas aeruginosa pao1

Structural highlights

3obb is a 1 chain structure with sequence from Pseudomonas aeruginosa. This structure supersedes the now removed PDB entries and 2h78. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
NonStd Res:
Gene:PA0743 (Pseudomonas aeruginosa)
Activity:Serine 3-dehydrogenase, with EC number 1.1.1.276
Resources:FirstGlance, OCA, RCSB, PDBsum

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 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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Tchigvintsev A, Singer A, Brown G, Flick R, Evdokimova E, Tan K, Gonzalez CF, Savchenko A, Yakunin AF. Biochemical and Structural Studies of Uncharacterized Protein PA0743 from Pseudomonas aeruginosa Revealed NAD+-dependent L-Serine Dehydrogenase. J Biol Chem. 2012 Jan 13;287(3):1874-83. Epub 2011 Nov 28. PMID:22128181 doi:10.1074/jbc.M111.294561

3obb, resolution 2.20Å

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