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| | ==Structural insights into substrate and cofactor selelction by sp2771== | | ==Structural insights into substrate and cofactor selelction by sp2771== |
| - | <StructureSection load='3vz1' size='340' side='right' caption='[[3vz1]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='3vz1' size='340' side='right'caption='[[3vz1]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vz1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Agmenellum_quadruplicatum Agmenellum quadruplicatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VZ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VZ1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vz1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_sp._PCC_7002 Synechococcus sp. PCC 7002]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VZ1 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vz0|3vz0]], [[3vz2|3vz2]], [[3vz3|3vz3]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SYNPCC7002_A2771 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32049 Agmenellum quadruplicatum])</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=3vz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vz1 OCA], [https://pdbe.org/3vz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vz1 RCSB], [https://www.ebi.ac.uk/pdbsum/3vz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vz1 ProSAT]</span></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=3vz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vz1 OCA], [http://pdbe.org/3vz1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vz1 RCSB], [http://www.ebi.ac.uk/pdbsum/3vz1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vz1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B1XMM6_SYNP2 B1XMM6_SYNP2] |
| | <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: Agmenellum quadruplicatum]] | + | [[Category: Large Structures]] |
| - | [[Category: Wei, D]] | + | [[Category: Synechococcus sp. PCC 7002]] |
| - | [[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: Oxidoreductase]]
| + | |
| - | [[Category: Substrate selection]]
| + | |
| Structural highlights
Function
B1XMM6_SYNP2
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.
See Also
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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