|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='4qyj' size='340' side='right'caption='[[4qyj]], [[Resolution|resolution]] 2.83Å' scene=''> | | <StructureSection load='4qyj' size='340' side='right'caption='[[4qyj]], [[Resolution|resolution]] 2.83Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qyj]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida_s12 Pseudomonas putida s12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QYJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QYJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qyj]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida_S12 Pseudomonas putida S12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QYJ FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RPPX_12610, RPPX_34495 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1215087 Pseudomonas putida S12])</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]] 2.83Å</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=4qyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qyj OCA], [http://pdbe.org/4qyj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qyj RCSB], [http://www.ebi.ac.uk/pdbsum/4qyj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qyj 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=4qyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qyj OCA], [https://pdbe.org/4qyj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qyj RCSB], [https://www.ebi.ac.uk/pdbsum/4qyj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qyj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/V4GH04_PSEPU V4GH04_PSEPU] |
| - | Phenylacetaldehyde dehydrogenase catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid in the styrene catabolic and detoxification pathway of Pseudomonas putida (S12). Here we report the structure and mechanistic properties of the N-terminally histidine-tagged enzyme, NPADH. The 2.83 A X-ray crystal structure is similar in fold to sheep liver cytosolic aldehyde dehydrogenase (ALDH1), but has unique set of intersubunit interactions and active site tunnel for substrate entrance. In solution, NPADH occurs as 227 kDa homotetramer. It follows a sequential reaction mechanism in which NAD+ serves as both the leading substrate and homotropic allosteric activator. In the absence of styrene monooxygenase reductase, which regenerates NAD+ from NADH in the first step of styrene catabolism, NPADH is inhibited by a ternary complex involving NADH, product, and phenylacetaldehyde, substrate. Each oligomerization domain of NPADH contains a six-residue insertion that extends this loop over the substrate entrance tunnel of a neighboring subunit, thereby obstructing the active site of the adjacent subunit. This feature could be an important factor in the homotropic activation and product inhibition mechanisms. Compared to ALDH1, the substrate channel of NPADH is narrower and lined with more aromatic residues, suggesting a means for enhancing substrate specificity.
| + | |
| - | | + | |
| - | Structure and biochemistry of phenylacetaldehyde dehydrogenase from the Pseudomonas putida S12 styrene catabolic pathway.,Crabo AG, Singh B, Nguyen T, Emami S, Gassner GT, Sazinsky MH Arch Biochem Biophys. 2017 Feb 15;616:47-58. doi: 10.1016/j.abb.2017.01.011. Epub, 2017 Jan 31. PMID:28153386<ref>PMID:28153386</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 4qyj" style="background-color:#fffaf0;"></div>
| + | |
| | | | |
| | ==See Also== | | ==See Also== |
| | *[[Aldehyde dehydrogenase 3D structures|Aldehyde dehydrogenase 3D structures]] | | *[[Aldehyde dehydrogenase 3D structures|Aldehyde dehydrogenase 3D structures]] |
| - | == References == | |
| - | <references/> | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseudomonas putida s12]] | + | [[Category: Pseudomonas putida S12]] |
| - | [[Category: Crabo, A G]] | + | [[Category: Crabo AG]] |
| - | [[Category: Gassner, G T]] | + | [[Category: Gassner GT]] |
| - | [[Category: Sazinsky, M H]] | + | [[Category: Sazinsky MH]] |
| - | [[Category: Aldehyde dehydrogenase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
