检索规则说明:AND代表“并且”;OR代表“或者”;NOT代表“不包含”;(注意必须大写,运算符两边需空一格)
检 索 范 例 :范例一: (K=图书馆学 OR K=情报学) AND A=范并思 范例二:J=计算机应用与软件 AND (U=C++ OR U=Basic) NOT M=Visual
作 者:姚文娟[1] 范文俊[1] 许小乐[1] 邓小昭[2] 张伟[1]
机构地区:[1]南通大学医学院,江苏南通226001 [2]南京军区军事医学研究所,江苏南京210002
出 处:《南通大学学报(自然科学版)》2012年第2期41-46,共6页Journal of Nantong University(Natural Science Edition)
基 金:江苏高校优势学科建设工程资助项目;南通市科技计划项目(AS2011020)
摘 要:利用ProtParam、TopPred、PredictProtein、PSORT-B Prediction、SWISS-MODEL等软件分别分析蛋白质的理化性质、跨膜区、二级结构、亚细胞定位、三维结构.结果显示:PgsB是亲水不稳定蛋白,通过豆蔻酰锚钩锚定于质膜上,催化作用需与ATP结合提供能量;PgsC是疏水稳定蛋白,通过4个跨膜区和多个豆蔻酰锚钩定位于质膜,具有酰胺化位点;PgsA是亲水稳定蛋白,通过N端一个跨膜区和豆蔻酰锚钩结合于质膜,具有多种磷酸化位点.说明γ-聚谷氨酸(Polyγ-glutamic acid,γ-PGA)合成酶系3个组分蛋白形成复合物定位于质膜上,其中PgsB在胞内催化γ-PGA合成,PgsC固定于质膜,连接PgsB和PgsA组分,PgsA在胞外负责γ-PGA的运输.通过对γ-PGA合成酶系各组分蛋白结构的分析,为日后在谷氨酸高产菌株中的表达奠定了基础.The physico-chemical properties,trans-membrane domains,secondary structures,sub-cellular localization and spatial structures are studied by ProtParam,TopPred,PredictProtein,PSORT-B Prediction and SWISS-MODEL,respectively.The results show that PgsB is a protein of hydrophilia and instability,and localizes to the membrane by myristoyl anchors.The catalytic action of PgsB requires combination of ATP to provide energy;PgsC is hydrophobic and stable,and localizes to the membrane by four trans-membrane domains and myristoyl anchors.PgsC has an amidation motif.PgsA is hydrophilic and stable,and localizes to the membrane by a trans-membrane domain in N terminus and myristoyl anchors.PgsC has many phosphorylation motifs.The results demonstrate that the compound of the three constituents from γ-PGA synthetase system is localized to the membrane.PgsB catalyzes γ-PGA synthesis.PgsC links PgsB and PgsA in the membrane.PgsA transports γ-PGA outside the cell.This study analyzes the structures of constituents from poly-γ-glutamate(γ-PGA) synthetase system in order to benefit expression of the synthetase system in the glutamate-producing strain.
正在载入数据...
正在载入数据...
正在载入数据...
正在载入数据...
正在载入数据...
正在载入数据...
正在载入数据...
正在链接到云南高校图书馆文献保障联盟下载...
云南高校图书馆联盟文献共享服务平台 版权所有©
您的IP:216.73.216.28