Hong Myoung-Ki, Lee Jae Jin, Wu Xing, Kim Jin-Kwang, Jeong Byeong Chul, Pham Tan-Viet, Kim Seung-Hwan, Lee Sang Hee, Kang Lin-Woo
Department of Advanced Technology Fusion, Konkuk University, Hwayang-dong, Gwangjin-gu, Seoul 143-701, Republic of Korea.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Sep 1;68(Pt 9):1124-7. doi: 10.1107/S1744309112033702. Epub 2012 Aug 31.
SFC-1, a class A carbapenemase that confers antibiotic resistance, hydrolyzes the β-lactam rings of β-lactam antibiotics (carbapenems, cephalosporins, penicillins and aztreonam). SFC-1 presents an enormous challenge to infection control, particularly in the eradication of Gram-negative pathogens. As SFC-1 exhibits a remarkably broad substrate range, including β-lactams of all classes, the enzyme is a potential target for the development of antimicrobial agents against pathogens producing carbapenemases. In this study, SFC-1 was cloned, overexpressed, purified and crystallized. The SFC-1 crystal diffracted to 1.6 Å resolution and belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 65.8, b = 68.3, c = 88.8 Å. Two molecules are present in the asymmetric unit, with a corresponding V(M) of 1.99 Å(3) Da(-1) and a solvent content of 38.1%.
SFC-1是一种赋予抗生素抗性的A类碳青霉烯酶,可水解β-内酰胺类抗生素(碳青霉烯类、头孢菌素类、青霉素类和氨曲南)的β-内酰胺环。SFC-1对感染控制构成了巨大挑战,尤其是在根除革兰氏阴性病原体方面。由于SFC-1表现出非常广泛的底物范围,包括所有类别的β-内酰胺,该酶是开发针对产生碳青霉烯酶的病原体的抗菌剂的潜在靶点。在本研究中,SFC-1被克隆、过表达、纯化并结晶。SFC-1晶体的衍射分辨率为1.6 Å,属于正交空间群P2(1)2(1)2(1),晶胞参数a = 65.8、b = 68.3、c = 88.8 Å。不对称单元中有两个分子,相应的V(M)为1.99 Å(3) Da(-1),溶剂含量为38.1%。