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| | <StructureSection load='1a4s' size='340' side='right'caption='[[1a4s]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='1a4s' size='340' side='right'caption='[[1a4s]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1a4s]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Gadus_callarias Gadus callarias]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A4S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1a4s]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Gadus_morhua_callarias Gadus morhua callarias]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A4S FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Betaine-aldehyde_dehydrogenase Betaine-aldehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.8 1.2.1.8] </span></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]] 2.1Å</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=1a4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4s OCA], [http://pdbe.org/1a4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a4s RCSB], [http://www.ebi.ac.uk/pdbsum/1a4s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a4s 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=1a4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4s OCA], [https://pdbe.org/1a4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a4s RCSB], [https://www.ebi.ac.uk/pdbsum/1a4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a4s ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AL9A1_GADMC AL9A1_GADMC] |
| | == 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: Betaine-aldehyde dehydrogenase]]
| + | [[Category: Gadus morhua callarias]] |
| - | [[Category: Gadus callarias]] | + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ahmad, M El]] | + | [[Category: Eklund H]] |
| - | [[Category: Eklund, H]] | + | [[Category: El Ahmad M]] |
| - | [[Category: Hjelmqvist, L]] | + | [[Category: Hjelmqvist L]] |
| - | [[Category: Johansson, K]] | + | [[Category: Johansson K]] |
| - | [[Category: Jornvall, H]] | + | [[Category: Jornvall H]] |
| - | [[Category: Ramaswamy, S]] | + | [[Category: Ramaswamy S]] |
| - | [[Category: Aldehyde oxidation]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
AL9A1_GADMC
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
The three-dimensional structure of betaine aldehyde dehydrogenase, the most abundant aldehyde dehydrogenase (ALDH) of cod liver, has been determined at 2.1 A resolution by the X-ray crystallographic method of molecular replacement. This enzyme represents a novel structure of the highly multiple ALDH, with at least 12 distinct classes in humans. This betaine ALDH of class 9 is different from the two recently determined ALDH structures (classes 2 and 3). Like these, the betaine ALDH structure has three domains, one coenzyme binding domain, one catalytic domain, and one oligomerization domain. Crystals grown in the presence or absence of NAD+ have very similar structures and no significant conformational change occurs upon coenzyme binding. This is probably due to the tight interactions between domains within the subunit and between subunits in the tetramer. The oligomerization domains link the catalytic domains together into two 20-stranded pleated sheet structures. The overall structure is similar to that of the tetrameric bovine class 2 and dimeric rat class 3 ALDH, but the coenzyme binding with the nicotinamide in anti conformation, resembles that of class 2 rather than of class 3.
Structure of betaine aldehyde dehydrogenase at 2.1 A resolution.,Johansson K, El-Ahmad M, Ramaswamy S, Hjelmqvist L, Jornvall H, Eklund H Protein Sci. 1998 Oct;7(10):2106-17. PMID:9792097[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Johansson K, El-Ahmad M, Ramaswamy S, Hjelmqvist L, Jornvall H, Eklund H. Structure of betaine aldehyde dehydrogenase at 2.1 A resolution. Protein Sci. 1998 Oct;7(10):2106-17. PMID:9792097 doi:10.1002/pro.5560071007
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