1nvm

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[[Image:1nvm.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of a bifunctional aldolase-dehydrogenase : sequestering a reactive and volatile intermediate==
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|PDB= 1nvm |SIZE=350|CAPTION= <scene name='initialview01'>1nvm</scene>, resolution 1.70&Aring;
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<StructureSection load='1nvm' size='340' side='right'caption='[[1nvm]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1nvm]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._CF600 Pseudomonas sp. CF600]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NVM FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetaldehyde_dehydrogenase_(acetylating) Acetaldehyde dehydrogenase (acetylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.10 1.2.1.10] </span>
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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]] 1.7&#8491;</td></tr>
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|GENE= DMPG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=306 Pseudomonas sp.]), DMPF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=306 Pseudomonas sp.])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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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=1nvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nvm OCA], [https://pdbe.org/1nvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nvm RCSB], [https://www.ebi.ac.uk/pdbsum/1nvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nvm ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nvm OCA], [http://www.ebi.ac.uk/pdbsum/1nvm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nvm RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/HOA_PSEUF HOA_PSEUF] Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of aromatic compounds such as phenols, cresols and catechols.[HAMAP-Rule:MF_01656]<ref>PMID:1732207</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/nv/1nvm_consurf.spt"</scriptWhenChecked>
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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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</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=1nvm ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of a bifunctional aldolase-dehydrogenase : sequestering a reactive and volatile intermediate'''
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==See Also==
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*[[Aldehyde dehydrogenase 3D structures|Aldehyde dehydrogenase 3D structures]]
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*[[Aldolase 3D structures|Aldolase 3D structures]]
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==Overview==
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== References ==
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The crystal structure of the bifunctional enzyme 4-hydroxy-2-ketovalerate aldolase (DmpG)/acylating acetaldehyde dehydrogenase (DmpF), which is involved in the bacterial degradation of toxic aromatic compounds, has been determined by multiwavelength anomalous dispersion (MAD) techniques and refined to 1.7-A resolution. Structures of the two polypeptides represent a previously unrecognized subclass of metal-dependent aldolases, and of a CoA-dependent dehydrogenase. The structure reveals a mixed state of NAD+ binding to the DmpF protomer. Domain movements associated with cofactor binding in the DmpF protomer may be correlated with channeling and activity at the DmpG protomer. In the presence of NAD+ a 29-A-long sequestered tunnel links the two active sites. Two barriers are visible along the tunnel and suggest control points for the movement of the reactive and volatile acetaldehyde intermediate between the two active sites.
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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1NVM is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NVM OCA].
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[[Category: Large Structures]]
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[[Category: Pseudomonas sp. CF600]]
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==Reference==
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[[Category: Manjasetty AB]]
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Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate., Manjasetty BA, Powlowski J, Vrielink A, Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):6992-7. Epub 2003 May 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12764229 12764229]
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[[Category: Powlowski J]]
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[[Category: Acetaldehyde dehydrogenase (acetylating)]]
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[[Category: Vrielink A]]
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[[Category: Protein complex]]
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[[Category: Pseudomonas sp.]]
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[[Category: Manjasetty, A B.]]
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[[Category: Powlowski, J.]]
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[[Category: Vrielink, A.]]
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[[Category: bifunctional enzyme]]
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[[Category: sequestered tunnel]]
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[[Category: substrate channeling]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:36:06 2008''
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Crystal structure of a bifunctional aldolase-dehydrogenase : sequestering a reactive and volatile intermediate

PDB ID 1nvm

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