1h5q

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[[Image:1h5q.png|left|200px]]
 
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==Mannitol dehydrogenase from Agaricus bisporus==
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The line below this paragraph, containing "STRUCTURE_1h5q", creates the "Structure Box" on the page.
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<StructureSection load='1h5q' size='340' side='right'caption='[[1h5q]], [[Resolution|resolution]] 1.50&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'>[[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>
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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]] 1.5&#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=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
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{{STRUCTURE_1h5q| PDB=1h5q | 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=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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MTDH_AGABI MTDH_AGABI]
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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/h5/1h5q_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=1h5q 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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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).
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===MANNITOL DEHYDROGENASE FROM AGARICUS BISPORUS===
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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>
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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_11335726}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1h5q" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11335726 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11335726}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[1h5q]] is a 12 chain structure with sequence from [http://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].
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==Reference==
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<ref group="xtra">PMID:11335726</ref><ref group="xtra">PMID:11320313</ref><references group="xtra"/>
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[[Category: Agaricus bisporus]]
[[Category: Agaricus bisporus]]
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[[Category: Baumann, U.]]
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[[Category: Large Structures]]
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[[Category: Horer, S.]]
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[[Category: Baumann U]]
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[[Category: Mooibroek, H.]]
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[[Category: Horer S]]
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[[Category: Sassoon, J.]]
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[[Category: Mooibroek H]]
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[[Category: Stoop, J.]]
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[[Category: Sassoon J]]
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[[Category: Mannitol metabolism]]
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[[Category: Stoop J]]
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[[Category: Oxidoreductase]]
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Current revision

Mannitol dehydrogenase from Agaricus bisporus

PDB ID 1h5q

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