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. 2011 Apr;79(4):1337-41.
doi: 10.1002/prot.22944. Epub 2011 Jan 18.

Structure of the C-terminal heme-binding domain of THAP domain containing protein 4 from Homo sapiens

Christopher M Bianchetti  1 , Craig A Bingman, George N Phillips Jr
Affiliations

Structure of the C-terminal heme-binding domain of THAP domain containing protein 4 from Homo sapiens

Christopher M Bianchetti et al. Proteins. 2011 Apr.
No abstract available

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Figures

Figure 1
Figure 1
A. Cartoon representation of cTHAP4 is shown going from blue at the N-terminus to red at the C-terminus. The bound heme is shown as sticks with carbon in white, nitrogen in blue, oxygen in red, and iron in orange. Looking down the barrel shows the heme coordinated by His567 and the extended hydrophobic cavity formed by the β-barrel. B. Structural alignment of the cTHAP4 dimer in green and the Nitrobindin dimer 14 (PDB ID 3EMM) in brown. Conserved hydrophobic residues that compose the dimer interface are shown as black sticks.
Figure 2
Figure 2
Sequence alignment of THAP4 from Mus musculus (Q6P3Z3), THAP4 from Rattus norvegicus (Q642B6), THAP4 from Homo sapiens (Q8WY91), THAP4 from Callithrix jacchus (A6MKW1), THAP4 from Bos taurus (Q2TBI2), Nitrobindin from Arabidopsis thaliana (O64527), uncharacterized protein from Vitis vinifera (A5BBZ0), fatty acid-binding like protein from Mycobacterium smegmatis (A0R6J8), and fatty acid-binding like protein from Mycobacterium vanbaalenii (A1T297). Residues that are within 4 A of the bound heme of cTHAP4 are highlighted in green. The strictly conserved histidine that coordinates the heme is highlighted in red.
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