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MBP-MalFGK_2相互作用动力学:ABC转运蛋白的模型研究

Dynamics Research on MBP-MalFGK_2 Interaction:ABC-Transport er Systems Model
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摘要 本文主要描述了麦芽糖结合蛋白(MBP)和属于ATP结合盒式蛋白(ABC)家族的麦芽糖转运蛋白复合物MalFGK2的相互作用。通过基因、结构和生化分析可知,MBP和MalFGK2以不同构象进行相互作用。在这个转运系统中,MBP与麦芽糖结合,并与MalFGK2发生相互作用,从而将麦芽糖从胞外转运至胞内,但由于MBP和MalFGK2都有多种构象,所以它们的相互作用很复杂。相互作用机理模型最重要的特点是结合配体的MBP,通过稳定MalFGK2的高能量构象来启动依赖ATP的麦芽糖转运过程。麦芽糖转运蛋白机理模型表明,ABC型转运系统利用外周结合蛋白,其转运过程基本上是不可逆的。 This article is focused on the interaction between maltose binding protein(MBP) and maltose trans porter complex,MalFGK2,which is a member of the ATP binding cassette(ABC) transporter superfamily.Through genetic,structural and biochemical analysis,the different conformation of MBP and MalFGK2 are described for in teractions.In the transport system,the maltose binding MBP and interact with MalFGK2,which transport maltose from the extracellular to intracellular,but MBP and MalFGK2 have multiple conformation,so their interaction is complex.The most important feature of interaction model is that ligand-bound MBP initiates the process of ATP-dependent maltose transport by stabilizing a high-energy conformation of MalFGK2.Maltose transporter mecha nism model show that the ABC transporter system makes use of the peripheral binding protein so that the trans port process is essentially irreversible.
出处 《生物技术通讯》 CAS 2012年第5期737-740,共4页 Letters in Biotechnology
基金 "十二五"国家科技重大专项 重大传染病应急处置检测技术平台(2011ZX10004-001)
关键词 ABC转运蛋白 麦芽糖结合蛋白 蛋白质相互作用 ATP水解 ABC transporter maltose binding protein protein-protein interaction ATP hydrolysis
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  • 1Nakanishi N, Shneider N, Axel R. A family of glutamate re- ceptor genes: evidence for the formation of heteromultimeric receptors with distinct channel properties[J]. Neuron, 1990,5: 569-581.
  • 2Acher F, Bertrand H. Amino acid recognition by Venus fly- trap domains is encoded in an 8-residue motil[J]. Biopoly- mers, 2005,80:357-366.
  • 3Murzin A G, Brenner S E, Hubbard T, et al. SCOP: a struc-tural classification of proteins database for the investigation of sequences and structures[J]. Mol Biol, 1995,247:536-540.
  • 4Kossmann M, Wolff C, Manson M D. Maltose chemoreceptor of Escherichia coli: interaction of mahose-binding protein and the tar signal transducer[J]. Bacteriology, 1985,170:4516-4521.
  • 5Bavoil P, Wandersman C, Schwartz M, et al. A mutant form of maltose-binding protein of Escherichia coli deficient in its interaction with the bacteriophage lambda receptor protein[J]. Bacteriology, 1983,155:919-921.
  • 6Luckey M, Nikaido H. Bacteriophage lambda receptor protein in Escherichia coli K-12: lowered affinity of some mutant pro- teins for maltose-binding protein in vitro[J]. Bacteriology, 1983,153:1056-1059.
  • 7Medintz I L, Deschamps J R. Mahose-binding protein: a ver- satile platform for prototypiag biosensing~J]. Curt" Opin Bioteeh- nol, 2006,17:17-27.
  • 8Sharff A J, Rodseth L E, Spurlino J C, et al. Crystallograph- ic evidence of a large ligand-induced hinge-twist motion be- tween the two domains of the maltodextrin binding protein in- volved in active transport and chemotaxis[J]. Biochemistry, 1992,31:10657-10663.
  • 9Duan X, Hall J A, Nikaido H, et al. Crystal structures of the mahodextrin/mahose-binding protein complexed with reduced oligosaccharides: flexibility of tertiary structure and ligand binding[J]. Mol Biol, 2001,306:1115-1126.
  • 10Duan X, Quiocho F A. Structural evidence for a dominant role of nonpolar interactions in the binding of a transport/che- mosensory receptor to its highly polar ligands[J]. Biochemis- try, 2002,41:706-712.

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