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  • 09월 10일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제124회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Structural analysis and substrate synthesis of peptidoglycan peptidase3, a metallopeptidase that control the shape of helical cell

2019년 8월 29일 16시 39분 27초
MEDI.P-283 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
10월 17일 (목요일) 11:00~12:30
Medicinal Chemistry
저자 및
Jisu Park, Byeong Moon Kim*, Se Won Suh*
Division of Chemistry, Seoul National University, Korea

Helicobacter pylori and Campylobacter jejuni, which are known to be helical shaped Gram-negative bacteria, colonize the human mucus layer of the gastrointestinal tract and cause various gastrointestinal diseases such as chronic gastritis, peptic ulcer, gastroenteritis and gastric adenocarcinoma in humans.1,2 In the pathogenesis and gut colonization, the helical shape of H. pylori and C. jejuni is believed to be a very important factor in their motility improvement.3 Recently, a series of genes associated with maintaining the helical cell shape in these bacteria have been identified, most of which have been found to encode for either endo- or exoproteases that act on the peptide chains of peptidoglycan.4 These proteases are referred to as cell shape determining (Csd) proteins or peptidoglycan peptides (Pgp). According to recent studies, inhibition of proteins responsible for the helical cell morphology could be useful in interference with the bacterial virulence and lifestyle, hence a very attractive therapeutic target.5 However, their catalytic processes and substrate recognition are largely unknown. In this study, we describe the synthesis of two substrates for Pgp3, one of the Csd proteins, and the analysis of the Pgp3-substrate complex structures of the active site of Pgp3 in high resolution.