 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 6]](uf5010fig6mag.jpg)
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Figure 6
Flexible structural elements of AcpS from M. smegmatis (msAcpS), M. tuberculosis (mtbAcpS) and C. ammoniagenes (caAcpS). (a) B-factor putty representation of the msAcpS, mtbAcpS (apo) and caAcpS (apo) structures. Regions with high structural flexibility have higher B factors and are represented in red with a large diameter. (b) Multiple sequence alignment of msAcpS, mtbAcpS and caAcpS. The loop connecting α3 and α4 is boxed in blue. The amino-acid sequence of this region is mostly similar in msAcpS and mtbAcpS except at the positions of Ser70, Lys71 and Gly79, which are replaced by Ala70, Gln71 and Asp79, respectively, in mtbAcpS, whereas in caAcpS the amino-acid sequence of this loop region is completely different. (c) Structural superposition showing that the flexibility of the loop connecting β2 to β3 is contributed by the binding position of the ligand. Upon ligand binding the position of Gly91 and Arg92 shifts forward to accommodate the adenine moiety of 3′,5′-ADP. |
![[Figure 6]](uf5010fig6.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
