Structural basis for a ribofuranosyl binding protein: insights into the furanose specific transport.
Structural basis for a ribofuranosyl binding protein: insights into the furanose specific transport.
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DOI：
10.1002/prot.22965
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发表时间：
2011-04
影响因子：
2.9
通讯作者：
Swaminathan, Subramanyam
中科院分区：
文献类型：
--
作者：
Bagaria, Ashima;Kumaran, Desigan;Burley, Stephen K.;Swaminathan, Subramanyam
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The ATP-binding cassette transporters (ABC-transporters) are members of one of the largest protein superfamilies, with representatives in all extant phyla1. These integral membrane proteins utilize the energy of ATP hydrolysis to carry out certain biological processes, including translocation of various substrates across membranes and non-transport related processes such as translation of RNA and DNA repair2. Typically, such transport systems in bacteria consist of an ATP binding component, a transmembrane permease, and a periplasmic receptor or binding protein.Soluble proteins found in the periplasm of gram-negative bacteria serve as the primary receptors for transport of many compounds, such as sugars, small peptides, and some ions. Ligand binding activates these periplasmic components, permitting recognition by the membrane spanning domain, which supports for transport and, in some cases, chemotaxis3-5. Transport and chemotaxis processes appear to be independent of one another, and a few mutants of bifunctional periplasmic components reveal the absence of one or the other function6.
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DOI：
10.1107/s0907444904019158
发表时间：
2004-12-01
影响因子：
2.2
作者：
Emsley, P;Cowtan, K
通讯作者：
Cowtan, K
影响因子：
5.6
作者：
Shilton, BH;Flocco, MM;Mowbray, SL
通讯作者：
Mowbray, SL
影响因子：
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作者：
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通讯作者：
Mowbray, SL
DOI：
10.1107/s0907444900005655
发表时间：
2000-07-01
期刊：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子：
--
作者：
Lin, DW;Manning, NO;Sussman, JL
通讯作者：
Sussman, JL
影响因子：
5.6
作者：
DUPLAY, P;SZMELCMAN, S;HOFNUNG, M
通讯作者：
HOFNUNG, M