1flg

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[[Image:1flg.jpg|left|200px]]
 
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==CRYSTAL STRUCTURE OF THE QUINOPROTEIN ETHANOL DEHYDROGENASE FROM PSEUDOMONAS AERUGINOSA==
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The line below this paragraph, containing "STRUCTURE_1flg", creates the "Structure Box" on the page.
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<StructureSection load='1flg' size='340' side='right'caption='[[1flg]], [[Resolution|resolution]] 2.60&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'>[[1flg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1eee 1eee]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FLG 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]] 2.6&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PQQ:PYRROLOQUINOLINE+QUINONE'>PQQ</scene></td></tr>
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{{STRUCTURE_1flg| PDB=1flg | 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=1flg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1flg OCA], [https://pdbe.org/1flg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1flg RCSB], [https://www.ebi.ac.uk/pdbsum/1flg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1flg ProSAT]</span></td></tr>
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</table>
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'''CRYSTAL STRUCTURE OF THE QUINOPROTEIN ETHANOL DEHYDROGENASE FROM PSEUDOMONAS AERUGINOSA'''
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== Function ==
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[https://www.uniprot.org/uniprot/QEDH_PSEAE QEDH_PSEAE] Catalyzes the oxidation of ethanol and other primary alcohols to the corresponding aldehydes, except methanol, which is a very poor substrate. Uses a specific inducible cytochrome c550, encoded by the adjacent gene in the locus, as electron acceptor. Is a key enzyme of the carbon and energy metabolism during growth of P.aeruginosa on ethanol as the sole carbon and energy source. Is also able to use secondary alcohols as well as aminoalcohols like ethanolamine and 1-amino-2-propanol, and aldehydes as substrates.<ref>PMID:19224199</ref> <ref>PMID:3144289</ref> <ref>PMID:8380982</ref>
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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The homodimeric enzyme form of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa ATCC 17933 crystallizes readily with the space group R3. The X-ray structure was solved at 2.6 A resolution by molecular replacement.Aside from differences in some loops, the folding of the enzyme is very similar to the large subunit of the quinoprotein methanol dehydrogenases from Methylobacterium extorquens or Methylophilus W3A1. Eight W-shaped beta-sheet motifs are arranged circularly in a propeller-like fashion forming a disk-shaped superbarrel. No electron density for a small subunit like that in methanol dehydrogenase could be found. The prosthetic group is located in the centre of the superbarrel and is coordinated to a calcium ion. Most amino acid residues found in close contact with the prosthetic group pyrroloquinoline quinone and the Ca(2+) are conserved between the quinoprotein ethanol dehydrogenase structure and that of the methanol dehydrogenases. The main differences in the active-site region are a bulky tryptophan residue in the active-site cavity of methanol dehydrogenase, which is replaced by a phenylalanine and a leucine side-chain in the ethanol dehydrogenase structure and a leucine residue right above the pyrrolquinoline quinone group in methanol dehydrogenase which is replaced by a tryptophan side-chain. Both amino acid exchanges appear to have an important influence, causing different substrate specificities of these otherwise very similar enzymes. In addition to the Ca(2+) in the active-site cavity found also in methanol dehydrogenase, ethanol dehydrogenase contains a second Ca(2+)-binding site at the N terminus, which contributes to the stability of the native enzyme.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fl/1flg_consurf.spt"</scriptWhenChecked>
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1FLG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1eee 1eee]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FLG OCA].
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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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==Reference==
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</jmolCheckbox>
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X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity., Keitel T, Diehl A, Knaute T, Stezowski JJ, Hohne W, Gorisch H, J Mol Biol. 2000 Apr 7;297(4):961-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10736230 10736230]
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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=1flg ConSurf].
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<div style="clear:both"></div>
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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]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Single protein]]
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[[Category: Diehl A]]
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[[Category: Diehl, A.]]
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[[Category: Gorisch H]]
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[[Category: Gorisch, H.]]
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[[Category: Hohne W]]
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[[Category: Hohne, W.]]
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[[Category: Keitel T]]
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[[Category: Keitel, T.]]
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[[Category: Knaute T]]
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[[Category: Knaute, T.]]
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[[Category: Stezowski JJ]]
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[[Category: Stezowski, J J.]]
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[[Category: Dehydrogenase]]
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[[Category: Quinoprotein]]
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[[Category: Superbarrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:27:48 2008''
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Current revision

CRYSTAL STRUCTURE OF THE QUINOPROTEIN ETHANOL DEHYDROGENASE FROM PSEUDOMONAS AERUGINOSA

PDB ID 1flg

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