Sandbox Reserved 1665

This Sandbox is Reserved from 01/25/2021 through 04/30/2021 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1665 through Sandbox Reserved 1682.

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Structure of Aldehyde Dehydrogenase C (AldC) mutant (C291A) from Pseudomonas syringae in complexed with NAD+ and Octanal

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Function of your protein My protein is important for agricultural reasons, as you can see from the amazing ligand that is bound to it. The protein in the article is Aldehyde dehydrogenase (AldC) and It has many functions. It helps with detoxification of aldehydes which are highly reactive compounds that are generated through cellular metabolism. It is also involved in biochemical functions from ethanol metabolism through oxidations, polyamine metabolism, and protective cellular response to stresses. The organism that is affection the protein is called Pseudomonas syringae (PtoDC3000) which is a mutation occurring in tomatoes. Biological relevance and broader implications The plant pathogen Pseudomonas syringae strain PtoDC3000 uses an indole-3-acetaldehyde dehydrogenase to synthesize the phytohormone indole-3-acetic acid to elude host responses. To suppress host defenses and promote diseases development, Pseudomonas syringae produces a variety of virulence factors, including phytohormones or chemical mimics of hormones, to manipulate hormone signaling in its host plants. P. syringae and many other plant-associated microbial pathogens can synthesize the major auxin indole-3-acetic acid (IAA), whose production is implicated in pathogen virulence. In this case the plant pathogen is affecting tomatoes, causing a mutation in them where the tomatoes dont have any defensed to fight off this plant pathogen. As mentioned in the article, there is a variety of pseudomonas species that have evolved to grow under unfavorable environmental conditions like for example sever nutrient limitations, extreme temperatures, high salinity, low oxygen or water availability. P. syringae, a species that includes many plant pathogenic strains, developed diverse bacterial virulence mechanisms to survive in the adverse environmental conditions of the phyllosphere. https://proteopedia.org/wiki/images/c/c9/AldC_Mutant_Site.PNG In this table we can see how the organism Pseudomonas syringae is affecting the protein AldC by stopping enzyme activities in the protein. In the NAD ligand is stops enzyme activities for C291A and K182A and for the octanal substrate it stops enzyme activities for N159A and L419A. This can be relevant to certain famers growing crops in different environments or climates. Pseudomonas syringae is a pathogen that can attack a wide variety of woody plant, it especially attacks them when the plants have been damaged by frost or an injury. Knowing this information farmers can be prepared so their crops are not affected by this pathogen. They can use a certain type of spray/chemical to protect them from it. Important amino acids 4 Catalytic Residues (Tetrad) (blue color) Asn 159, Glu 257, Gly 288, Cys 291(Cys 291 mutates to Ala 291) NAD+ Ligand (binding site, 19 residues) Ile 155, Asn 159, Lys 182, Gly 219, Ile 233-Ser 236, Ala 239, Leu 242, Glu 257, Leu 258, Gly 259, Cys 291, Glu 391, Phe 393 Octanal Ligand (binding site) Trp 160, Tyr 163, Trp 450, Phe 456, Tyr 458, Met 114, Leu 118 In the article, there were other substrates mentioned that were detected in AldC by using spectrophotometric assay. Substrates that were identified were aliphatic aldehydes of 5–9-carbon length, like hydrocinnamaldehyde and 4-pyridinecarboxyaldehyde. As substrates, octanal had the highest specific activity that function properly for AldC. The article also mentions that short 2–4-carbon aldehydes, branched aliphatic aldehydes, and larger aromatic aldehydes are poor substrates for AldC. https://proteopedia.org/wiki/images/3/3a/AldC_activie_sites.PNG (In the figure above it shows the active sites for AldC) Red color indicated a hydrophobic interaction White color indicates a polar interaction Side chains interacting with Octanal are green Side chains interacting with NAD are blue. There are two water molecules (red spheres) interacting with the cofactor NAD Hydrogen bonds interactions between amino acid residues and ligands are in yellow Structural highlights Secondary structure has feature and domains, the N-terminus of the protein contains a central Beta sheet that is surrounded by alpha helices to form the NAD(H)-binding site. Around the C-Terminus end of the protein it consists a mix of alpha/beta domains, which include a catalytic cysteine residue and forms the aldehyde -binding site. The article mentions as well what connects the N and C terminal domains of the protein AldC is by an interdomain linker region. https://proteopedia.org/wiki/images/3/32/Aldehyde_dehydrogenage_of_AldC.PNG The enzyme functions primarily as a long-chained aliphatic aldehyde dehydrogenase. The biochemical activity of AldC from PtoDC3000 is consistent with the traditional role of aldehyde dehydrogenases as metabolic clean-up enzymes that convert reactive aldehydes into less active carboxylates. Other important features This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.