Structural characterization and comparison of three acyl-carrier-protein synthases from pathogenic bacteria

Halavaty, A.S.; Kim, Y.; Minasov, G.; Shuvalova, L.; Dubrovska, I.; Winsor, J.; Zhou, M.; Onopriyenko, O.; Skarina, T.; Papazisi, L.; Kwon, K.; Peterson, S.N.; Joachimiak, A.; Savchenko, A.; Anderson, W.F.

doi:10.1107/S0907444912029101

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 5
Structural comparison of bacterial AcpS. (a) Surface diagram of the sequence-based structural alignment of the bacterial AcpS enzymes presented in Fig. 1

(a). The structure of apo-AcpS_SA is used to display the conservation of the residues, which are colored from blue (variable) to red (100% conserved). The positions of two 3′,5′-ADP molecules (black) in AcpS_BA and of CoA (white) in AcpS_VC are shown. (b) Stereogram of the monomer–monomer interaction interface in the AcpS_SA trimer. Residues are colored from blue (variable) to red (100% conserved). The third molecule is omitted for clarity. (c) Stereogram of the least-squares superposition of the AcpS_SA (red), AcpS_VC (blue) and AcpS_BA (green) structures.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 68| Part 10| October 2012| Pages 1359-1370

https://doi.org/10.1107/S0907444912029101

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