2bmm
From Proteopedia
|
X-RAY STRUCTURE OF A NOVEL THERMOSTABLE HEMOGLOBIN FROM THE ACTINOBACTERIUM THERMOBIFIDA FUSCA
Overview
The gene coding for a hemoglobin-like protein (Tf-trHb) has been, identified in the thermophilic actinobacterium Thermobifida fusca and, cloned in Escherichia coli for overexpression. The crystal structure of, the ferric, acetate-bound derivative, was obtained at 2.48 A resolution., The three-dimensional structure of Tf-trHb is similar to structures, reported for the truncated hemoglobins from Mycobacterium tuberculosis and, Bacillus subtilis in its central domain. The complete lack of diffraction, patterns relative to the N- and C-terminal segments indicates that these, are unstructured polypeptides chains, consistent with their facile, cleavage in solution. The absence of internal cavities and the presence of, two water molecules between the bound acetate ion and the protein surface, ... [(full description)]
About this Structure
2BMM is a [Single protein] structure of sequence from [Thermobifida fusca] with ACT and HEM as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
A novel thermostable hemoglobin from the actinobacterium Thermobifida fusca., Bonamore A, Ilari A, Giangiacomo L, Bellelli A, Morea V, Boffi A, FEBS J. 2005 Aug;272(16):4189-201. PMID:16098200
Page seeded by OCA on Tue Oct 30 16:42:38 2007
