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Homology modeling of the spatial structure of HydSL hydrogenase from purple sulphur bacterium Thiocapsa roseopersicina BBS
Computer Research and Modeling, 2013, v. 5, no. 4, pp. 737-747Views (last year): 2. Citations: 5 (RSCI).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.
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International Interdisciplinary Conference "Mathematics. Computing. Education"