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. Author manuscript; available in PMC: 2014 Apr 9.
Published in final edited form as: Nat Struct Mol Biol. 2012 Feb 19;19(3):358–360. doi: 10.1038/nsmb.2251

Figure 2.

Figure 2

TbpB stabilizes the holo form of hTf. A The cartoon representation of the buried His349 from hTf in contact with His143, Asp159, Lys206 from TbpB illustrates their interaction through a tetra-coordinated bridging water within the binding interface. The four residues and the tetrahedral coordinated water (red sphere) are embedded within a simulated annealing 2Fo-Fc electron density map at 1.0 sigma missing the hTf His349 residue. Domains colored as in figure 1a (cyan, yellow and blue denote the C1 and C2 hTf domains and the N-lobe TbpB handle domain, respectively). B The schematic model of the tetra-coordinated water is shown with structure-based predicted pKa values for each residue indicated.