Sandbox Reserved 1670: Difference between revisions
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== Function of your protein == | == Function of your protein == | ||
This protein is from | 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. | ||
== Biological relevance and broader implications == | == 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. | |||
== Important amino acids== | == Important amino acids== | ||
The protein | |||
== Structural highlights == | == Structural highlights == | ||
<scene name='87/873232/Protein_structure/2'>Protein Structure</scene> | <scene name='87/873232/Protein_structure/2'>Protein Structure</scene> | ||
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<scene name='87/873232/Mutated_catalytic_tetrad/3'>Mutated Catalytic Tetrad</scene> | <scene name='87/873232/Mutated_catalytic_tetrad/3'>Mutated Catalytic Tetrad</scene> | ||
The structure of AldC is a homodimer, this means that the protein has two identical chains that are joined together. | |||
