2I4C
Crystal structure of Bicarbonate Transport Protein CmpA from Synechocystis sp. PCC 6803 in complex with bicarbonate and calcium
2I4C の概要
エントリーDOI | 10.2210/pdb2i4c/pdb |
関連するPDBエントリー | 2I48 2I49 2I4B |
分子名称 | Bicarbonate transporter, BICARBONATE ION, CALCIUM ION, ... (4 entities in total) |
機能のキーワード | alpha-beta protein, c-clamp, periplasmic solute-binding protein, abc transporter, bicarbonate, transport protein |
由来する生物種 | Synechocystis sp. |
細胞内の位置 | Cell inner membrane; Peripheral membrane protein (By similarity): Q55460 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 47186.96 |
構造登録者 | |
主引用文献 | Koropatkin, N.M.,Koppenaal, D.W.,Pakrasi, H.B.,Smith, T.J. The Structure of a Cyanobacterial Bicarbonate Transport Protein, CmpA. J.Biol.Chem., 282:2606-2614, 2007 Cited by PubMed Abstract: Cyanobacteria, blue-green algae, are the most abundant autotrophs in aquatic environments and form the base of the food chain by fixing carbon and nitrogen into cellular biomass. To compensate for the low selectivity of Rubisco for CO2 over O2, cyanobacteria have developed highly efficient CO2-concentrating machinery of which the ABC transport system CmpABCD from Synechocystis PCC 6803 is one component. Here, we have described the structure of the bicarbonate-binding protein CmpA in the absence and presence of bicarbonate and carbonic acid. CmpA is highly homologous to the nitrate transport protein NrtA. CmpA binds carbonic acid at the entrance to the ligand-binding pocket, whereas bicarbonate binds in nearly an identical location compared with nitrate binding to NrtA. Unexpectedly, bicarbonate binding is accompanied by a metal ion, identified as Ca2+ via inductively coupled plasma optical emission spectrometry. The binding of bicarbonate and metal appears to be highly cooperative and suggests that CmpA may co-transport bicarbonate and calcium or that calcium acts a cofactor in bicarbonate transport. PubMed: 17121816DOI: 10.1074/jbc.M610222200 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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