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. Author manuscript; available in PMC: 2011 Aug 24.
Published in final edited form as: Biochemistry. 2010 Aug 24;49(33):7060–7068. doi: 10.1021/bi100866b

Figure 2.

Figure 2

The hemerythrin domain of P1B-5-ATPases. Top: Alignment of eight representative P1B-5-Hr sequences with the Hr domain of DcrH (DcrH-Hr, GI 887858, UniProtKB Q46583). The metal-binding residues of DcrH-Hr along with corresponding residues from P1B-5-Hrs are colored with histidine in green, glutamic acid in orange, and aspartic acid in violet. The red helices below the sequence correspond to the known secondary structure elements of DcrH-Hr. The P1B-5-Hr sequences correspond to the following proteins: S. viridochromogenes, GI 256799641; M. vanbaalenii, GI 120402396, UniProtKB A1T4W9; R. erythropolis, GI 226306903, UniProtKB C1A0I9; B. phymatum, GI 186471018, UniProtKB B2JWG3; B. dolosa, GI 254255483, UniProtKB A2WJ24; M. nodulans, GI 220919964, UniProtKB B8IWI5; A. cellulolyticus, GI 117927237, UniProtKB A0LQU2; R. vannielii, GI 283824493, UniProtKB D2LJH3. Bottom: The structure of the diiron center in the azide adduct of DcrH-Hr (PDB accession code 2AVK).