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The protein being studied in this article is KGP. This cysteine peptidase is a major virulence factor for the periodontopathogen Porphyromonas gingivalis. KGP works by cleaving many constituents of human connective tissue which leads to decreased bacterial activity and chronic inflammation in the gums. It contains a catalytic triad of cysteine histidine and aspartic acid. The histidine and aspartic acid residues in the catalytic triad use acid base chemistry catalysis to form a covalent intermediate with the cysteine. The intermediate formed is L-lysinylmethyl which is found in the specificity pocket.
Disease
Porphyromonas gingivalis is a Gram-Negative oral anaerobe that leads to periodontitis. It invades periodontal tissues, and evades the host defense mechanisms by a series of virulence factors, such as KGP, that deregulate innate immune and inflammatory responses. This bacteria and its products can enter circulation and contribute to the development of diabetes, cardiovascular disease, and rheumatoid arthritis.
Relevance
Bacteria are typically beneficial to maintaining a healthy mouth, however, if they are a susceptible host they can become pathogenic. Once they become pathogenic they can invade tissues and lead to infection and disease. Resistant strains are currently responsible for half of all infections, and resistant pathogens infect over 2 million people annually in the United States. The only way to keep up with these resistant pathogens is by developing new antimicrobials, but the pharmaceutical industry is failing to keep up. By studying KGP, scientists hope to find a suitable inhibitor to eliminate KGP activity, and thus prevent periodontal disease in humans.
Structural highlights
The of KGP is made up of about equal amounts of alpha helices and antiparallel beta sheets.
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