3gdg
From Proteopedia
(Difference between revisions)
m (Protected "3gdg" [edit=sysop:move=sysop]) |
|||
(6 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | [[Image:3gdg.png|left|200px]] | ||
- | < | + | ==Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum.== |
- | + | <StructureSection load='3gdg' size='340' side='right'caption='[[3gdg]], [[Resolution|resolution]] 2.30Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[3gdg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cladosporium_herbarum Cladosporium herbarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GDG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GDG 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]] 2.3Å</td></tr> | |
- | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=3gdg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gdg OCA], [https://pdbe.org/3gdg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gdg RCSB], [https://www.ebi.ac.uk/pdbsum/3gdg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gdg ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/MTDH_DAVTA MTDH_DAVTA] | ||
+ | == 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/gd/3gdg_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=3gdg ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The ascomycete Cladosporium herbarum is a prominent fungal inducer of Type I allergy. The only major allergen identified so far is Cla h 8, a NADP-dependent mannitol dehydrogenase (MtDH). MtDH, a cytoplasmic protein of 28.5kDa, belongs to the Short chain Dehydrogenases/Reductases (SDR), acting as a NADP-dependent oxidoreductase. In this study, we found that C. herbarum MtDH can exist as monomers, dimers and tetramers in solution and, correspondingly, forms tetramers and higher oligomers in two crystal structures. Additionally, we identified a unique adaptive binding site for the metal ions Na(+) and Zn(2+) that were distinguished by an anomalous dispersion experiment. A Translation-Libration-Screw analysis confirmed the stabilising effect of Zn(2+) for the tetrameric assembly. Moreover, the zinc containing structure explains the mode of MtDH multimerisation by metal bridging of the tetramers. The formation of oligomers and higher multimers of MtDH provides a missing link to its allergenic properties. Based on the well defined active site region and a comparative analysis with related structures, we can also clarify the atypical enzymatic properties of MtDH by two alternative binding modes of the substrate to the active site. | ||
- | + | Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum: Implications for oligomerisation and catalysis.,Nuss D, Goettig P, Magler I, Denk U, Breitenbach M, Schneider PB, Brandstetter H, Simon-Nobbe B Biochimie. 2010 Aug;92(8):985-93. Epub 2010 Apr 24. PMID:20420880<ref>PMID:20420880</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 3gdg" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | [[Category: Cladosporium herbarum]] |
- | + | [[Category: Large Structures]] | |
- | + | [[Category: Brandstetter H]] | |
- | == | + | [[Category: Breitenbach M]] |
- | < | + | [[Category: Denk U]] |
- | [[Category: | + | [[Category: Goettig P]] |
- | [[Category: Brandstetter | + | [[Category: Magler I]] |
- | [[Category: Breitenbach | + | [[Category: Nuess D]] |
- | [[Category: Denk | + | [[Category: Schneider PB]] |
- | [[Category: Goettig | + | [[Category: Simon-Nobbe B]] |
- | [[Category: Magler | + | |
- | [[Category: Nuess | + | |
- | [[Category: Schneider | + | |
- | [[Category: Simon-Nobbe | + | |
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + |
Current revision
Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum.
|