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| | ==Structural insights into cofactor and substrate selection by Gox0499== | | ==Structural insights into cofactor and substrate selection by Gox0499== |
| - | <StructureSection load='3vz0' size='340' side='right' caption='[[3vz0]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='3vz0' size='340' side='right'caption='[[3vz0]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vz0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Gluox Gluox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VZ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VZ0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vz0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Gluconobacter_oxydans_621H Gluconobacter oxydans 621H]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VZ0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</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]] 2.3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vz1|3vz1]], [[3vz2|3vz2]], [[3vz3|3vz3]]</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=3vz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vz0 OCA], [https://pdbe.org/3vz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vz0 RCSB], [https://www.ebi.ac.uk/pdbsum/3vz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vz0 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GOX0499 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=290633 GLUOX])</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=3vz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vz0 OCA], [http://pdbe.org/3vz0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vz0 RCSB], [http://www.ebi.ac.uk/pdbsum/3vz0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vz0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5FTL8_GLUOX Q5FTL8_GLUOX] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Gluox]] | + | [[Category: Gluconobacter oxydans 621H]] |
| - | [[Category: Wei, D]] | + | [[Category: Large Structures]] |
| - | [[Category: Yin, B]] | + | [[Category: Wei D]] |
| - | [[Category: Yuan, Y A]] | + | [[Category: Yin B]] |
| - | [[Category: Yuan, Z]] | + | [[Category: Yuan YA]] |
| - | [[Category: Cofactor preference]] | + | [[Category: Yuan Z]] |
| - | [[Category: Gox0499]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Substrate selection]]
| + | |
| Structural highlights
Function
Q5FTL8_GLUOX
Publication Abstract from PubMed
Aldehyde dehydrogenase (ALDH) catalyzes the oxidation of aldehydes to carboxylic acids. Cyanobacterium Synechococcus contains one ALDH enzyme (Sp2771), together with a novel 2-oxoglutarate decarboxylase, to complete a non-canonical tricarboxylic acid cycle. However, the molecular mechanisms for substrate selection and cofactor preference by Sp2771 are largely unknown. Here, we report crystal structures of wild type Sp2771, Sp2771 S419A mutant and ternary structure of Sp2771 C262A mutant in complex with NADP(+) and SSA, as well as binary structure of Gluconobacter oxydans aldehyde dehydrogenase (Gox0499) in complex with PEG. Structural comparison of Sp2771 with Gox0499, coupled with mutational analysis, demonstrates that Ser157 residue in Sp2771 and corresponding Pro159 residue in Gox0499 play critical structural roles in determining NADP(+) and NAD(+) preference for Sp2771 and Gox0499, respectively, whereas size and distribution of hydrophobic residues along the substrate binding funnel determine substrate selection. Hence, our work has provided insightful structural information into cofactor and substrate selection by ALDH.
Structural basis for cofactor and substrate selection by cyanobacterium succinic semialdehyde dehydrogenase.,Yuan Z, Yin B, Wei D, Yuan YR J Struct Biol. 2013 May;182(2):125-35. doi: 10.1016/j.jsb.2013.03.001. Epub 2013 , Mar 13. PMID:23500184[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yuan Z, Yin B, Wei D, Yuan YR. Structural basis for cofactor and substrate selection by cyanobacterium succinic semialdehyde dehydrogenase. J Struct Biol. 2013 May;182(2):125-35. doi: 10.1016/j.jsb.2013.03.001. Epub 2013 , Mar 13. PMID:23500184 doi:10.1016/j.jsb.2013.03.001
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