Structure prediction and docking study of RpiA from extremophile Acidithiobacillus ferrooxidans
The gene RpiA from Acidithiobacillus ferrooxidans may play a crucial role in the CO2 fixation of this organism. To investigate the protein encoded by this gene, a reliable three-dimensional molecular structure of it was built. The obtained structure was further used to search binding sites, to carry out flexible docking with the substrate Ribose -5 phosphate (R5P) , and hereby detect its key residues. In this docking complex, the residues of Asp81, Thr31, Lysl21, Ser30, Glul03, Asp84, Lys94, Aspll8, Lys7 and H2O have large interaction energies and/or hydrogen bonds fixation with R5P, which are well consistent with those experimental facts of the homologues from other sources. Moreover, the other four residues of Gly97 , Gly29, Gly95 and Thr28 also have large interaction energies with R5P, which are fitly conserved in Ribose —5 —phosphate isomerase A (RpiA) proteins from all kinds of sources, but have not been identified before. According to these results, this gene encodes the RpiA; The substrate R5P can be effectively recruited into the active pocket; The above detected key residues are directly responsible for the bind and/or catalysis of R5P.
ribose - 5 - phosphate isomerase A (RpiA) Acidithiobacillus ferrooxidans homology modeling docking Ribose - 5 - phosphate (R5P)
Yuandong Liu Guanzhou Qiu
School of Minerals Processing and Bioengineering, Central South University, 410083, Changsha, China Key Laboratory of Biometallurgy of Ministry of Education, Cental South University, 410083, Changsha, China
国际会议
The 19th International Biohydrometallurgy Symposium(第19届国际生物湿法冶金大会 IBS2011)
长沙
英文
393-399
2011-09-18（万方平台首次上网日期，不代表论文的发表时间）