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1m2w

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(New page: 200px<br /><applet load="1m2w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m2w, resolution 1.80&Aring;" /> '''Pseudomonas fluoresc...)
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[[Image:1m2w.jpg|left|200px]]<br /><applet load="1m2w" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1m2w, resolution 1.80&Aring;" />
 
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'''Pseudomonas fluorescens mannitol 2-dehydrogenase ternary complex with NAD and D-mannitol'''<br />
 
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==Overview==
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==Pseudomonas fluorescens mannitol 2-dehydrogenase ternary complex with NAD and D-mannitol==
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Long-chain mannitol dehydrogenases are secondary alcohol dehydrogenases, that are of wide interest because of their involvement in metabolism and, potential applications in agriculture, medicine, and industry. They differ, from other alcohol and polyol dehydrogenases because they do not contain a, conserved tyrosine and are not dependent on Zn(2+) or other metal, cofactors. The structures of the long-chain mannitol 2-dehydrogenase (54, kDa) from Pseudomonas fluorescens in a binary complex with NAD(+) and, ternary complex with NAD(+) and d-mannitol have been determined to, resolutions of 1.7 and 1.8 A and R-factors of 0.171 and 0.176, respectively. These results show an N-terminal domain that includes a, typical Rossmann fold. The C-terminal domain is primarily alpha-helical, and mediates mannitol binding. The electron lone pair of Lys-295 is, steered by hydrogen-bonding interactions with the amide oxygen of Asn-300, and the main-chain carbonyl oxygen of Val-229 to act as the general base., Asn-191 and Asn-300 are involved in a web of hydrogen bonding, which, precisely orients the mannitol O2 proton for abstraction. These residues, also aid in stabilizing a negative charge in the intermediate state and in, preventing the formation of nonproductive complexes with the substrate., The catalytic lysine may be returned to its unprotonated state using a, rectifying proton tunnel driven by Glu-292 oscillating among different, environments. Despite low sequence homology, the closest structural, neighbors are glycerol-3-phosphate dehydrogenase, N-(1-d-carboxylethyl)-l-norvaline dehydrogenase, UDP-glucose, dehydrogenase, and 6-phosphogluconate dehydrogenase, indicating a possible, evolutionary relationship among these enzymes.
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<StructureSection load='1m2w' size='340' side='right'caption='[[1m2w]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1m2w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M2W 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]] 1.8&#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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=MTL:D-MANNITOL'>MTL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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=1m2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m2w OCA], [https://pdbe.org/1m2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m2w RCSB], [https://www.ebi.ac.uk/pdbsum/1m2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m2w ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O08355_PSEFL O08355_PSEFL]
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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/m2/1m2w_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=1m2w ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1M2W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens] with NAD and MTL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Mannitol_2-dehydrogenase Mannitol 2-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.67 1.1.1.67] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M2W OCA].
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*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase binary and ternary complexes. Specificity and catalytic mechanism., Kavanagh KL, Klimacek M, Nidetzky B, Wilson DK, J Biol Chem. 2002 Nov 8;277(45):43433-42. Epub 2002 Aug 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12196534 12196534]
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[[Category: Large Structures]]
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[[Category: Mannitol 2-dehydrogenase]]
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[[Category: Pseudomonas fluorescens]]
[[Category: Pseudomonas fluorescens]]
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[[Category: Single protein]]
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[[Category: Kavanagh KL]]
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[[Category: Kavanagh, K.L.]]
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[[Category: Klimacek M]]
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[[Category: Klimacek, M.]]
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[[Category: Nidetzky B]]
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[[Category: Nidetzky, B.]]
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[[Category: Wilson DK]]
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[[Category: Wilson, D.K.]]
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[[Category: MTL]]
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[[Category: NAD]]
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[[Category: di-nucleotide binding motif]]
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[[Category: long-chain dehydrogenase]]
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[[Category: polyol dehydrogenase]]
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[[Category: rossmann fold]]
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[[Category: secondary alcohol dehydrogenase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:42:18 2007''
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Current revision

Pseudomonas fluorescens mannitol 2-dehydrogenase ternary complex with NAD and D-mannitol

PDB ID 1m2w

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