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| | ==Histamine dehydrogenase from Nocardiodes simplex== | | ==Histamine dehydrogenase from Nocardiodes simplex== |
| - | <StructureSection load='3k30' size='340' side='right' caption='[[3k30]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='3k30' size='340' side='right'caption='[[3k30]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3k30]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"corynebacterium_simplex"_jensen_1934 "corynebacterium simplex" jensen 1934]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3K30 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3k30]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pimelobacter_simplex Pimelobacter simplex]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K30 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hadh, hdh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2045 "Corynebacterium simplex" Jensen 1934])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3k30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k30 OCA], [http://pdbe.org/3k30 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k30 RCSB], [http://www.ebi.ac.uk/pdbsum/3k30 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3k30 ProSAT]</span></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=3k30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k30 OCA], [https://pdbe.org/3k30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k30 RCSB], [https://www.ebi.ac.uk/pdbsum/3k30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k30 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6IWJ5_NOCSI Q6IWJ5_NOCSI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Corynebacterium simplex jensen 1934]] | + | [[Category: Large Structures]] |
| - | [[Category: Limburg, J]] | + | [[Category: Pimelobacter simplex]] |
| - | [[Category: Reed, T M]] | + | [[Category: Limburg J]] |
| - | [[Category: Scott, E E]] | + | [[Category: Reed TM]] |
| - | [[Category: 6-s-cysteinyl-fmn]] | + | [[Category: Scott EE]] |
| - | [[Category: Adp binding site]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
Q6IWJ5_NOCSI
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Histamine dehydrogenase (HADH) isolated from Nocardioides simplex catalyzes the oxidative deamination of histamine to imidazole acetaldehyde. HADH is highly specific for histamine, and we are interested in understanding the recognition mode of histamine in its active site. We describe the first crystal structure of a recombinant form of HADH (HADH) to 2.7-A resolution. HADH is a homodimer, where each 76-kDa subunit contains an iron-sulfur cluster ([4Fe-4S](2+)) and a 6-S-cysteinyl flavin mononucleotide (6-S-Cys-FMN) as redox cofactors. The overall structure of HADH is very similar to that of trimethylamine dehydrogenase (TMADH) from Methylotrophus methylophilus (bacterium W3A1). However, some distinct differences between the structure of HADH and TMADH have been found. Tyr(60), Trp(264), and Trp(355) provide the framework for the "aromatic bowl" that serves as a trimethylamine-binding site in TMADH is comprised of Gln(65), Trp(267), and Asp(358), respectively, in HADH. The surface Tyr(442) that is essential in transferring electrons to electron-transfer flavoprotein (ETF) in TMADH is not conserved in HADH. We use this structure to propose the binding mode for histamine in the active site of HADH through molecular modeling and to compare the interactions to those observed for other histamine-binding proteins whose structures are known.
Crystal structure of histamine dehydrogenase from Nocardioides simplex.,Reed T, Lushington GH, Xia Y, Hirakawa H, Travis DM, Mure M, Scott EE, Limburg J J Biol Chem. 2010 Aug 13;285(33):25782-91. Epub 2010 Jun 10. PMID:20538584[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Reed T, Lushington GH, Xia Y, Hirakawa H, Travis DM, Mure M, Scott EE, Limburg J. Crystal structure of histamine dehydrogenase from Nocardioides simplex. J Biol Chem. 2010 Aug 13;285(33):25782-91. Epub 2010 Jun 10. PMID:20538584 doi:10.1074/jbc.M109.084301
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