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. Author manuscript; available in PMC: 2008 Aug 21.
Published in final edited form as: Biochemistry. 2007 May 17;46(23):6830–6843. doi: 10.1021/bi7002263

Figure 1.

Figure 1

Top: Ribbon drawing of the NP4-NO structure. The loops that move on NO binding (loop A-B, residues 31-37 and loop G-H, residues 125-132) are colored red, the heme is cyan (stick representation), the disulfide bonds are yellow, and the linear NO representation in blue and red (ball and stick representation). The N-terminal A residue is seen at the top, just before the first disulfide bond. Bottom: Hydrogen bonding in the mobile loops of NP4. a) Stereo view of the distal pocket in NP4-NO. b) Stereo view of the N-terminus in NP4-NO. In a) and b), bonds are open for Asp 30 and filled for the other residues. Nitrogens are indicated by large open spheres, carbons by small open spheres, oxygens by shaded spheres, and hydrogen bonds by dashed lines. Reprinted from reference 25 with permission of Nature.