 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 5]](sw5008fig5mag.jpg)
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Figure 5
(a) An alignment of the amino-acid sequence of SaCMK with those of CMK from E. coli (EcCMK) and S. pneumoniae (SpCMK), drawn with ESPRIPT (Gouet et al., 1999  ). Residues are boxed according to an alignment made with ClustalW (Thompson et al., 1994; SwissProt IDs P63807, Q97PK6 and P0A6I0 for SaCMK, SpCMK and EcCMK sequences, respectively). Residues that are strictly conserved have a red background, residues that are well conserved are indicated by red lettering and the remainder are in black. The secondary-structure elements of SaCMK are presented at the top: α-helices by squiggles and β-strands by arrows. The positions of the P-loop, the NMP-binding domain and the LID domain of SaCMK are indicated below the alignment. (b) A ribbon representation showing the superposition of the SaCMK–CMP (coloured red), EcCMK–CMP (blue) and apo SpCMK (green) complexes. The figure was prepared using PyMOL. |
![[Figure 5]](sw5008fig5.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
