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Figure 1
(a) Domain architecture of Bem3 and cartoon representation of the PX and PH domains of Bem3 and their relative positions within the full-length protein. Important regions that are putatively involved in membrane binding are indicated for both domains. The inset additionally shows a magnified view of β4PH where the electron density did not allow unambiguous assignment of the amino-acid side chains (2mFoDFc electron density shown in black at an r.m.s.d. of 1). Therefore, the anomalous signal from the SeMet-derivative crystals was used to correctly assign the position of amino acids (anomalous map in magenta depicted at an r.m.s.d. of 4). (b) Electrostatic potential of Bem3 contoured at ±5kT e−1 calculated with APBS (Baker et al., 2001BB3) shown in two orientations including the highly basic putative membrane-binding site [the upper figure is shown in the same orientation as in (a), the membrane is indicated below the structure]. All structural representations were prepared with PyMOL (DeLano & Lam, 2005BB9). (c) Sequence alignment produced with PROMALS3D (Pei et al., 2008BB34) of Bem3 with the PX domain of Ncf1 (UniProt ID P14598) and the PH domain of PLCδ (UniProt ID P10688). Important residues that belong to the basic motifs I and II (PX domain; Sato et al., 2001BB38) and the PIP-binding region within the PH domain (Lemmon, 2007BB25) are highlighted in red.

ISSN: 2053-230X
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