1m2w

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[[Image:1m2w.png|left|200px]]
 
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==Pseudomonas fluorescens mannitol 2-dehydrogenase ternary complex with NAD and D-mannitol==
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The line below this paragraph, containing "STRUCTURE_1m2w", creates the "Structure Box" on the page.
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<StructureSection load='1m2w' size='340' side='right'caption='[[1m2w]], [[Resolution|resolution]] 1.80&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'>[[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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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]] 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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{{STRUCTURE_1m2w| PDB=1m2w | 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=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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== 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/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=1m2w 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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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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===Pseudomonas fluorescens mannitol 2-dehydrogenase ternary complex with NAD and D-mannitol===
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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:12196534<ref>PMID:12196534</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_12196534}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1m2w" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12196534 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12196534}}
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==About this Structure==
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[[1m2w]] is a 2 chain structure of [[Alcohol dehydrogenase]] with sequence from [http://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].
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==See Also==
==See Also==
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*[[Alcohol dehydrogenase]]
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*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:012196534</ref><references group="xtra"/>
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__TOC__
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[[Category: Mannitol 2-dehydrogenase]]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pseudomonas fluorescens]]
[[Category: Pseudomonas fluorescens]]
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[[Category: Kavanagh, K L.]]
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[[Category: Kavanagh KL]]
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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, D K.]]
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[[Category: Wilson DK]]
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[[Category: Di-nucleotide binding motif]]
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[[Category: Long-chain dehydrogenase]]
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[[Category: Oxidoreductase]]
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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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Current revision

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

PDB ID 1m2w

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