1kv9

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(New page: 200px<br /><applet load="1kv9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kv9, resolution 1.9&Aring;" /> '''Structure at 1.9 A Re...)
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[[Image:1kv9.jpg|left|200px]]<br /><applet load="1kv9" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1kv9, resolution 1.9&Aring;" />
 
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'''Structure at 1.9 A Resolution of a Quinohemoprotein Alcohol Dehydrogenase from Pseudomonas putida HK5'''<br />
 
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==Overview==
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==Structure at 1.9 A Resolution of a Quinohemoprotein Alcohol Dehydrogenase from Pseudomonas putida HK5==
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The type II quinohemoprotein alcohol dehydrogenase of Pseudomonas putida, is a periplasmic enzyme that oxidizes substrate alcohols to the aldehyde, and transfers electrons first to pyrroloquinoline quinone (PQQ) and then, to an internal heme group. The 1.9 A resolution crystal structure reveals, that the enzyme contains a large N-terminal eight-stranded beta propeller, domain (approximately 60 kDa) similar to methanol dehydrogenase and a, small C-terminal c-type cytochrome domain (approximately 10 kDa) similar, to the cytochrome subunit of p-cresol methylhydoxylase. The PQQ is bound, near the axis of the propeller domain about 14 A from the heme. A molecule, of acetone, the product of the oxidation of isopropanol present during, crystallization, appears to be bound in the active site cavity.
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<StructureSection load='1kv9' size='340' side='right'caption='[[1kv9]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1kv9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KV9 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]] 1.9&#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=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=PQQ:PYRROLOQUINOLINE+QUINONE'>PQQ</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=1kv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kv9 OCA], [https://pdbe.org/1kv9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kv9 RCSB], [https://www.ebi.ac.uk/pdbsum/1kv9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kv9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/QHED_PSEPU QHED_PSEPU] Catalyzes the dye-linked oxidation of primary alcohols to the corresponding aldehydes and the (subsequent) oxidation of the aldehydes to carboxylic acids. Exhibits activity with longer mono-alcohols (C-4 to C-7) but not with methanol or glycerol. Reacts with 1,2-propanediol and 1,3-propanediol but not with sugar alcohols such as D-sorbitol.<ref>PMID:10320337</ref> <ref>PMID:18218017</ref> <ref>PMID:7730276</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/kv/1kv9_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=1kv9 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 type II quinohemoprotein alcohol dehydrogenase of Pseudomonas putida is a periplasmic enzyme that oxidizes substrate alcohols to the aldehyde and transfers electrons first to pyrroloquinoline quinone (PQQ) and then to an internal heme group. The 1.9 A resolution crystal structure reveals that the enzyme contains a large N-terminal eight-stranded beta propeller domain (approximately 60 kDa) similar to methanol dehydrogenase and a small C-terminal c-type cytochrome domain (approximately 10 kDa) similar to the cytochrome subunit of p-cresol methylhydoxylase. The PQQ is bound near the axis of the propeller domain about 14 A from the heme. A molecule of acetone, the product of the oxidation of isopropanol present during crystallization, appears to be bound in the active site cavity.
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==About this Structure==
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Structure at 1.9 A resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5.,Chen ZW, Matsushita K, Yamashita T, Fujii TA, Toyama H, Adachi O, Bellamy HD, Mathews FS Structure. 2002 Jun;10(6):837-49. PMID:12057198<ref>PMID:12057198</ref>
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1KV9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with CA, PQQ, HEM, EPE, ACN and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KV9 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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Structure at 1.9 A resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5., Chen ZW, Matsushita K, Yamashita T, Fujii TA, Toyama H, Adachi O, Bellamy HD, Mathews FS, Structure. 2002 Jun;10(6):837-49. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12057198 12057198]
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</div>
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[[Category: Pseudomonas putida]]
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<div class="pdbe-citations 1kv9" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Adachi, O.]]
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[[Category: Bellamy, H.D.]]
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[[Category: Chen, Z.W.]]
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[[Category: Fujii, T.]]
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[[Category: Mathews, F.S.]]
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[[Category: Matsushita, K.]]
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[[Category: Toyama, H.]]
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[[Category: Yamashita, T.]]
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[[Category: ACN]]
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[[Category: CA]]
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[[Category: EPE]]
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[[Category: GOL]]
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[[Category: HEM]]
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[[Category: PQQ]]
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[[Category: electron transfer]]
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[[Category: quinohemoprotein alcohol dehydrogenase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:00:30 2007''
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==See Also==
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*[[Alcohol dehydrogenase 3D structures|Alcohol 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: Pseudomonas putida]]
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[[Category: Adachi O]]
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[[Category: Bellamy HD]]
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[[Category: Chen Z-W]]
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[[Category: Fujii T]]
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[[Category: Mathews FS]]
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[[Category: Matsushita K]]
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[[Category: Toyama H]]
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[[Category: Yamashita T]]

Current revision

Structure at 1.9 A Resolution of a Quinohemoprotein Alcohol Dehydrogenase from Pseudomonas putida HK5

PDB ID 1kv9

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