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. Author manuscript; available in PMC: 2015 Jul 1.
Published in final edited form as: Biochemistry. 2013 Apr 11;52(16):2705–2707. doi: 10.1021/bi400280z

Figure 2.

Figure 2

(A) Structure of apo-HasAyp tet with the Q32 loop shown in magenta and the Y75 loop in cyan; Q32, Y75 and H81 are shown in sticks. (B) Superimposed structures of apo-HasAp (PDB ID: 3MOK) and apo-HasAyp tet where the H32 loop in apo-HasAp is shown in coral and the Q32 loop in apo-HasAyp tet in magenta. (C) The structure of holo-HasAyp is very similar to that of apo-HasAyp; the Q32 loop is in green and the Y75 loop in cyan. (D) Superposition of holo-HasAyp and holo-HasAp (PDB ID: 3ELL) structures. The hemin iron in HasAp is coordinated by Y75 and H32, whereas in holo-HasAyp it is coordinated by Y75 (also see Figure 3). (E) Zoomed-in view comparing the heme-binding pockets of holo-HasAyp (green) and holo-HasAp (orange); a chloride ion (purple sphere) in the distal pocket of HasAyp is in the position occupied by the side chain of H32 in holo-HasAp and holo-HasAsm. Structures were superimposed using the program Superpose (16).