Homology modeling of the spatial structure of HydSL hydrogenase from purple sulphur bacterium Thiocapsa roseopersicina BBS

Abdullatypov A.V., Tsygankov A.A.
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The results of homology modeling of HydSL, a NiFe-hydrogenase from purple sulphur bacterium Thiocapsa roseopersicina BBS are presented in this work. It is shown that the models have larger confidence level than earlier published ones; a full-size model of HydSL hydrogenase is presented for the first time. The C-end fragment of the enzyme is shown to have random orientation in relation to the main protein globule. The obtain models have a large number of ion pairs, as well as thermostable HydSL hydrogenase from Allochromatium vinosum, in contrast to thermolabile HydAB hydrogenase from Desulfovibrio vulgaris.

Keywords: homology modeling, hydrogenases, Thiocapsa roseopersicina
Citation in English: Abdullatypov A.V., Tsygankov A.A. Homology modeling of the spatial structure of HydSL hydrogenase from purple sulphur bacterium Thiocapsa roseopersicina BBS // Computer Research and Modeling, 2013, vol. 5, no. 4, pp. 737-747
Citation in English: Abdullatypov A.V., Tsygankov A.A. Homology modeling of the spatial structure of HydSL hydrogenase from purple sulphur bacterium Thiocapsa roseopersicina BBS // Computer Research and Modeling, 2013, vol. 5, no. 4, pp. 737-747
DOI: 10.20537/2076-7633-2013-5-4-737-747
URL: http://crm-en.ics.org.ru/journal/article/2079/
Creative Commons License This work is licensed under a Creative Commons Attribution-NoDerivs 3.0 Unported License.
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  • A. V. Abdullatypov, A. A. Tsygankov. Modeling three-dimensional structure of two closely related Ni–Fe hydrogenases. // Photosynthesis Research. — 2015. — V. 125, no. 1-2. — P. 341. DOI: 10.1007/s11120-014-0071-z
  • A. V. Abdullatypov, N. A. Zorin, A. A. Tsygankov. Interaction of HydSL hydrogenase from the purple sulfur bacterium Thiocapsa roseopersicina BBS with methyl viologen and positively charged polypeptides. // Biochemistry (Moscow). — 2014. — V. 79, no. 8. — P. 805. DOI: 10.1134/S0006297914080082
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