Evidence for a Two-Metal-Ion Mechanism in the Cytidyltransferase KdsB, an Enzyme Involved in Lipopolysaccharide Biosynthesis
文献类型：期刊论文
| 作者 | Schmidt, Helgo2; Mesters, Jeroen R.2; Wu, Jing3; Woodard, Ronald W.3; Hilgenfeld, Rolf1,2,4; Mamat, Uwe5 |
| 刊名 | PLOS ONE
 |
| 出版日期 | 2011-08-03 |
| 卷号 | 6期号:8 |
| ISSN号 | 1932-6203 |
| DOI | 10.1371/journal.pone.0023231 |
| 文献子类 | Article |
| 英文摘要 | Lipopolysaccharide (LPS) is located on the surface of Gram-negative bacteria and is responsible for maintaining outer membrane stability, which is a prerequisite for cell survival. Furthermore, it represents an important barrier against hostile environmental factors such as antimicrobial peptides and the complement cascade during Gram-negative infections. The sugar 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) is an integral part of LPS and plays a key role in LPS functionality. Prior to its incorporation into the LPS molecule, Kdo has to be activated by the CMP-Kdo synthetase (CKS). Based on the presence of a single Mg2+ ion in the active site, detailed models of the reaction mechanism of CKS have been developed previously. Recently, a two-metal-ion hypothesis suggested the involvement of two Mg2+ ions in Kdo activation. To further investigate the mechanistic aspects of Kdo activation, we kinetically characterized the CKS from the hyperthermophilic organism Aquifex aeolicus. In addition, we determined the crystal structure of this enzyme at a resolution of 2.10 angstrom and provide evidence that two Mg2+ ions are part of the active site of the enzyme. |
| WOS关键词 | CMP-2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE ; CMP-KDO SYNTHETASE ; ESCHERICHIA-COLI ; NEISSERIA-MENINGITIDIS ; 8-PHOSPHATE SYNTHASE ; CATALYTIC MECHANISM ; CYTIDYLYLTRANSFERASE ; COMPLEXES ; PURIFICATION ; POLYMERASES |
| 资助项目 | Deutsche Forschungsgemeinschaft (DFG)[MA 1408/2-1] ; Deutsche Forschungsgemeinschaft (DFG)[ME 2741/1-1] ; Deutsche Forschungsgemeinschaft (DFG)[EXC 306] ; EC[LSH2005-037793] ; National Institutes of Health[AI1061531] ; Chinese Academy of Sciences[2010T1S6] ; Fonds der Chemischen Industrie[00000000] |
| WOS研究方向 | Science & Technology - Other Topics |
| 语种 | 英语 |
| WOS记录号 | WOS:000293558900068 |
| 出版者 | PUBLIC LIBRARY SCIENCE |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/278447]  |
| 专题 | 中国科学院上海药物研究所 |
| 通讯作者 | Schmidt, Helgo |
| 作者单位 | 1.Chinese Acad Sci, Shanghai Inst Mat Med, Shanghai 200031, Peoples R China; 2.Univ Lubeck, Inst Biochem, Ctr Struct & Cell Biol Med, Lubeck, Germany; 3.Univ Michigan, Coll Pharm, Dept Med Chem, Ann Arbor, MI 48109 USA; 4.DESY, Lab Struct Biol Infect & Inflammat, D-2000 Hamburg, Germany; 5.Leibniz Ctr Med & Biosci, Res Ctr Borstel, Div Struct Biochem, Borstel, Germany |
| 推荐引用方式 GB/T 7714 | Schmidt, Helgo,Mesters, Jeroen R.,Wu, Jing,et al. Evidence for a Two-Metal-Ion Mechanism in the Cytidyltransferase KdsB, an Enzyme Involved in Lipopolysaccharide Biosynthesis[J]. PLOS ONE,2011,6(8). |
| APA | Schmidt, Helgo,Mesters, Jeroen R.,Wu, Jing,Woodard, Ronald W.,Hilgenfeld, Rolf,&Mamat, Uwe.(2011).Evidence for a Two-Metal-Ion Mechanism in the Cytidyltransferase KdsB, an Enzyme Involved in Lipopolysaccharide Biosynthesis.PLOS ONE,6(8). |
| MLA | Schmidt, Helgo,et al."Evidence for a Two-Metal-Ion Mechanism in the Cytidyltransferase KdsB, an Enzyme Involved in Lipopolysaccharide Biosynthesis".PLOS ONE 6.8(2011). |
入库方式： OAI收割
来源：上海药物研究所
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