Sandbox Reserved 1670

Text To Be Displayed

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.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing

Structure of Aldehyde dehydrogenase

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 This protein can be found in the plant pathogenic microbe Pseudomonas syringae strain PtoDC3000. The p. syringae mutautes its host, which in this case is tomato. The p. syringae produces a toxin that cause the tomato to not be able to fight off, there for causing diseases in the tomato. The research focuses on aldehyde dehydrogenases specifically aldC. aldehyde dehydrogenases are known for its capability to detoxing aldehydes, this is important because aldehydes are very reactive, so for an example from the article they can be turned into carboxylic acids which are not as reactive, which I believe slows down the mutation. The substrate of the AldC PtoDC3000 shows that this enzyme functions as a long-chain aliphatic aldehyde dehydrogenase. This article states that they ran tests to find the best substrate for this enzyme, which they found multiple substrate such as aliphatic aldehydes of 5–9-carbon length, as well as hydrocinnamaldehyde and 4-pyridinecarboxyaldehyde but it shows that octanal has the highest activity. Biological relevance and broader implications Learning about the mutant and its host is relevant because it can affect the food supply, which as humans we need. Studying this mutant will give us an understanding on what the mutation is and if it can be avoided. This research can lead the farming industry to a solution to the mutant. There are many chemicals that can be found being used with crops such as weed killers and fertilizers. Important amino acids NAD+ binding site has 19 catalytic residues which consist of Ile155–Asn159, Lys182, Gly219, Ile233–Ser236, Ala239, Leu242, Glu257, Leu258, Gly259, Cys291, Glu391, and Phe393 4 catalytic amino acids known as the Catalytic Tetrad consisting of Asn159, Glu257, Gly288, and Cys291. Cys291 can be found to be mutated to an Ala Mutated Catalytic Tetrad There are two ligands in each of the chains in the homodimer NAD and Octanal The mutation of C291A can be found in the middle of the two ligands affecting the binding efficiency of the structure. C291A mutation with ligand Structural highlights Protein Structure NAD and Octanal Catalytic Tetrad Mutated Catalytic Tetrad The structure is made up of about 60% alpha helices and 30% beta sheets and 10% of other structures like water. The shape of this structure looks like its split in two bulbs with a narrow middle part, this is because it is a homodimer. It has two identical chains (A and B) covalently bonded together. You can also find two ligands in each side of the structure. This is a structure to highlight the ligand of the protein while everything else is transparent. This is to show the main structure while highlighting the interaction with the ligand. ligands The ligands that can be found in the structure are octanal and NAD+. Other important features NEED TO REWORD THIS The secondary structure features and domains of the AldC monomer are similar to those of other aldehyde dehydrogenase family members The C-terminal region consists of a mixed a/b domain, which includes the catalytic cysteine residue and forms the aldehyde-binding site" "The N-terminal Rossmann-fold domain contains a central b-sheet (b9-b8-b7- b10-b11) surrounded by a-helices to form the NAD(H)-binding site"