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![[Figure 3]](hv5284fig3mag.jpg)
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Figure 3
Structure of monomeric actin. (a) Monomeric P. falciparum actin I (PDB entry 4cbu ; Vahokoski et al., 2014  ). The regions with the largest differences from α-actin (PDB entry 1eqy
; McLaughlin et al., 1993) are indicated with a red hue in the background. Colour-coding of the protein is as in Fig. 2. ATP is shown as sticks and the bound Ca2+ ion is shown as a grey sphere. The subdomains are numbered and the N- and C-termini as well as the general actin-binding protein binding cleft and the D-loop are labelled. (b) Comparison of the active-site details of P. falciparum actin I (green) and α-actin (grey). Tyr337 of actin I is in a double conformation. Residue 17 is an asparagine in actin I and a leucine in α-actin. Residue numbering follows that of P. falciparum actin I. (c) Conformational changes in the active site of α-actin upon ATP hydrolysis. ATP state, PDB entry 1nwk
(Graceffa & Dominguez, 2003; grey); ADP state, PDB entry 1j6z
(Otterbein et al., 2001; magenta). Residue 17 is a leucine in both structures. For clarity, the residue numbering follows that of P. falciparum actin I, as in (b). |
![[Figure 3]](hv5284fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
