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N.Nakano, N.Okazaki, S.Satoh, K.Takio, S.Kuramitsu, A.Shinkai, S.Yokoyama. (2006). Structure of the stand-alone RAM-domain protein from Thermus thermophilus HB8. Acta Crystallograph Sect F Struct Biol Cryst Commun, 62, 855-860. [PubMed id: 16946463]
Figure 3.
Figure 3 Schematic representation of the overall fold of the T. thermophilus SraA protein. (a) The dimeric structure (subunits A and F). The colour coding is the same as in Fig. 1-. (b) The decameric structure. Subunits A-J are indicated. Zinc ions in the asymmetric unit are coloured grey. (c) Stereoview of the zinc-binding site. A zinc ion interacts with Glu50 and Asp54 of helix 2 in subunit B and Glu20 of helix 1 in subunit A of the neighbouring ring. These figures were prepared using MOLSCRIPT (Kraulis, 1991[Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.]) and RASTER3D (Merritt & Murphy, 1994[Merritt, E. A. & Murphy, M. E. P. (1994). Acta Cryst. D50, 869-873.]).
Figure 4.
Figure 4 (a) The Asp39 residues of SraA are coloured green on a ribbon diagram of the decameric ring. The side-chain atoms of Asp39 are represented by a ball-and-stick model. This figure was prepared with MOLSCRIPT (Kraulis, 1991[Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.]). (b) The Asp39 residues are represented on the surface of the tetrameric SraA molecule composed of the AF (yellow) and BG (white) dimers. This figure was prepared using PyMOL ( ).
Figures reprinted by permission from the IUCr: Acta Crystallograph Sect F Struct Biol Cryst Commun (2006, 62, 855-860) copyright 2006.
PDB entries for which this is a key reference: 2djw.
M.Goel, P.Anuradha, K.J.Kaur, B.G.Maiya, M.J.Swamy, D.M.Salunke. (2004). Porphyrin binding to jacalin is facilitated by the inherent plasticity of the carbohydrate-binding site: novel mode of lectin-ligand interaction. Acta Crystallogr D Biol Crystallogr, 60, 281-288. [PubMed id: 14747704]
Figure 1.
Figure 1 Stereo drawing of the molecular packing of jacalin-H[2]TPPS in the unit cell as viewed along the crystallographic a axis. A stack of porphyrin molecules interacting with two independent molecules of jacalin leads to extensive cross-linking of the jacalin molecules.
Figure 6.
Figure 6 Comparison of porphyrin juxtaposed with (a) jacalin and (b) ConA in the corresponding carbohydrate-binding sites. Porphyrin is shown in sticks (blue) and jacalin and ConA, incorporating the corresponding sandwiched water molecules, are molecular-surface representations coloured according to charge (red, negative; blue, positive).
Figures reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2004, 60, 281-288) copyright 2004.
PDB entries for which this is a key reference: 1pxd.
T.Wan, R.L.Beavil, S.M.Fabiane, A.J.Beavil, M.K.Sohi, M.Keown, R.J.Young, A.J.Henry, R.J.Owens, H.J.Gould, B.J.Sutton. (2002). The crystal structure of IgE Fc reveals an asymmetrically bent conformation. Nat Immunol, 3, 681-686. [PubMed id: 12068291]
Figure 1.
Figure 1. Domain structure of IgE Fc.
Figure 2.
Figure 2. Asymmetry in the contacts between each of the C 2 domains and the C 3 and C 4 domains.
Figures reprinted by permission from Macmillan Publishers Ltd: Nat Immunol (2002, 3, 681-686) copyright 2002.
PDB entries for which this is a key reference: 1ls0, 1o0v.
PDB entries for which this is a secondary reference: 2wqr, 2y7q.
S.Tassin-Moindrot, A.Caille, J.P.Douliez, D.Marion, F.Vovelle. (2000). The wide binding properties of a wheat nonspecific lipid transfer protein. Solution structure of a complex with prostaglandin B2. Eur J Biochem, 267, 1117-1124. [PubMed id: 10672021]
Figure 3.
Fig. 3. Superposition of the backbone of the 12 NMR conformers of the protein (light grey) and of the heavy atoms of the ligand (dark grey).
Figure 4.
Fig. 4. The wheat ns-LTP/PGB[2] complex. (A) The protein is shown as a tube structure with the four helices coloured in cyan. The ligand is shown as CPK representation and O atoms of the ligand are coloured in magenta. (B) The hydrophobic cavity of the liganded protein in which PGB[2] has been deleted.
Figures reprinted by permission from the Federation of European Biochemical Societies: Eur J Biochem (2000, 267, 1117-1124) copyright 2000.
PDB entries for which this is a key reference: 1cz2.