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| | <StructureSection load='2euh' size='340' side='right'caption='[[2euh]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='2euh' size='340' side='right'caption='[[2euh]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2euh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_25175 Atcc 25175]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EUH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2euh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EUH FirstGlance]. <br> |
| - | </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=SO4:SULFATE+ION'>SO4</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]] 2.6Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(NADP(+)) Glyceraldehyde-3-phosphate dehydrogenase (NADP(+))], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.9 1.2.1.9] </span></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=SO4:SULFATE+ION'>SO4</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=2euh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2euh OCA], [https://pdbe.org/2euh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2euh RCSB], [https://www.ebi.ac.uk/pdbsum/2euh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2euh 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=2euh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2euh OCA], [https://pdbe.org/2euh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2euh RCSB], [https://www.ebi.ac.uk/pdbsum/2euh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2euh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/GAPN_STRMU GAPN_STRMU] |
| | == 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: Atcc 25175]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aubry, A]] | + | [[Category: Streptococcus mutans]] |
| - | [[Category: Branlant, G]] | + | [[Category: Aubry A]] |
| - | [[Category: Cobessi, D]] | + | [[Category: Branlant G]] |
| - | [[Category: Marchal, S]] | + | [[Category: Cobessi D]] |
| - | [[Category: Tete-Favier, F]] | + | [[Category: Marchal S]] |
| - | [[Category: Dehydrogenase]]
| + | [[Category: Tete-Favier F]] |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
GAPN_STRMU
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 aldehyde dehydrogenases (ALDHs) are a superfamily of multimeric enzymes which catalyse the oxidation of a broad range of aldehydes into their corresponding carboxylic acids with the reduction of their cofactor, NAD or NADP, into NADH or NADPH. At present, the only known structures concern NAD-dependent ALDHs. Three structures are available in the Protein Data Bank: two are tetrameric and the other is a dimer. We solved by molecular replacement the first structure of an NADP-dependent ALDH isolated from Streptococcus mutans, in its apo form and holo form in complex with NADP, at 1.8 and 2.6 A resolution, respectively. Although the protein sequence shares only approximately 30 % identity with the other solved tetrameric ALDHs, the structures are very similar. However, a large local conformational change in the region surrounding the 2' phosphate group of the adenosine moiety is observed when the enzyme binds NADP, in contrast to the NAD-dependent ALDHs.Structure and sequence analyses reveal several properties. A small number of residues seem to determine the oligomeric state. Likewise, the nature (charge and volume) of the residue at position 180 (Thr in ALDH from S. mutans) determines the cofactor specificity in comparison with the structures of NAD-dependent ALDHs. The presence of a hydrogen bond network around the cofactor not only allows it to bind to the enzyme but also directs the side-chains in a correct orientation for the catalytic reaction to take place. Moreover, a specific part of this network appears to be important in substrate binding. Since the enzyme oxidises the same substrate, glyceraldehyde-3-phosphate (G3P), as NAD-dependent phosphorylating glyceraldehyde-3-phosphate dehydrogenases (GAPDH), the active site of GAPDH was compared with that of the S. mutans ALDH. It was found that Arg103, Arg283 and Asp440 might be key residues for substrate binding.
Apo and holo crystal structures of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans.,Cobessi D, Tete-Favier F, Marchal S, Azza S, Branlant G, Aubry A J Mol Biol. 1999 Jul 2;290(1):161-73. PMID:10388564[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cobessi D, Tete-Favier F, Marchal S, Azza S, Branlant G, Aubry A. Apo and holo crystal structures of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans. J Mol Biol. 1999 Jul 2;290(1):161-73. PMID:10388564 doi:10.1006/jmbi.1999.2853
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