1h5q
From Proteopedia
(Difference between revisions)
(New page: 200px<br /> <applet load="1h5q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h5q, resolution 1.50Å" /> '''MANNITOL DEHYDROGEN...) |
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| - | [[Image:1h5q.gif|left|200px]]<br /> | ||
| - | <applet load="1h5q" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1h5q, resolution 1.50Å" /> | ||
| - | '''MANNITOL DEHYDROGENASE FROM AGARICUS BISPORUS'''<br /> | ||
| - | == | + | ==Mannitol dehydrogenase from Agaricus bisporus== |
| - | Mannitol, an acyclic six-carbon polyol, is one of the most abundant sugar | + | <StructureSection load='1h5q' size='340' side='right'caption='[[1h5q]], [[Resolution|resolution]] 1.50Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1h5q]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Agaricus_bisporus Agaricus bisporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H5Q FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h5q OCA], [https://pdbe.org/1h5q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h5q RCSB], [https://www.ebi.ac.uk/pdbsum/1h5q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h5q ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MTDH_AGABI MTDH_AGABI] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h5/1h5q_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1h5q ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Mannitol, an acyclic six-carbon polyol, is one of the most abundant sugar alcohols occurring in nature. In the button mushroom, Agaricus bisporus, it is synthesized from fructose by the enzyme mannitol 2-dehydrogenase (MtDH; EC ) using NADPH as a cofactor. Mannitol serves as the main storage carbon (up to 50% of the fruit body dry weight) and plays a critical role in growth, fruit body development, osmoregulation, and salt tolerance. Furthermore, mannitol dehydrogenases are being evaluated for commercial mannitol production as alternatives to the less efficient chemical reduction of fructose. Given the importance of mannitol metabolism and mannitol dehydrogenases, MtDH was cloned into the pET28 expression system and overexpressed in Escherichia coli. Kinetic and physicochemical properties of the recombinant enzyme are indistinguishable from the natural enzyme. The crystal structure of its binary complex with NADP was solved at 1.5-A resolution and refined to an R value of 19.3%. It shows MtDH to be a tetramer and a member of the short chain dehydrogenase/reductase family of enzymes. The catalytic residues forming the so-called catalytic triad can be assigned to Ser(149), Tyr(169), and Lys(173). | ||
| - | + | The crystallographic structure of the mannitol 2-dehydrogenase NADP+ binary complex from Agaricus bisporus.,Horer S, Stoop J, Mooibroek H, Baumann U, Sassoon J J Biol Chem. 2001 Jul 20;276(29):27555-61. Epub 2001 May 2. PMID:11335726<ref>PMID:11335726</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1h5q" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Agaricus bisporus]] | [[Category: Agaricus bisporus]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Baumann | + | [[Category: Baumann U]] |
| - | [[Category: Horer | + | [[Category: Horer S]] |
| - | [[Category: Mooibroek | + | [[Category: Mooibroek H]] |
| - | [[Category: Sassoon | + | [[Category: Sassoon J]] |
| - | [[Category: Stoop | + | [[Category: Stoop J]] |
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Current revision
Mannitol dehydrogenase from Agaricus bisporus
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