3MYO

Crystal structure of tagatose-1,6-bisphosphate aldolase from Streptococcus pyogenes

Summary for 3MYO

• Entry DOI: 10.2210/pdb3myo/pdb
• Related: 3MYP
• Descriptor: Tagatose 1,6-diphosphate aldolase 1 (2 entities in total)
• Functional Keywords: beta-alpha-barrel, lyase
• Biological source: Streptococcus pyogenes
• Total number of polymer chains: 2
• Total formula weight: 74237.57

Authors

Lee, S.J.,Kim, H.S.,Kim, D.J.,Yoon, H.J.,Kim, K.H.,Yoon, J.Y.,Suh, S.W. (deposition date: 2010-05-10, release date: 2011-01-26, Last modification date: 2023-11-01)

Primary citation

Lee, S.J.,Kim, H.S.,Kim, D.J.,Yoon, H.J.,Kim, K.H.,Yoon, J.Y.,Suh, S.W.
Crystal structures of LacD from Staphylococcus aureus and LacD.1 from Streptococcus pyogenes: Insights into substrate specificity and virulence gene regulation
Febs Lett., 585:307-312, 2011

PubMed Abstract: Staphylococcus aureus LacD, a Class I tagatose-1,6-bisphosphate (TBP) aldolase, shows broadened substrate specificity by catalyzing the cleavage of 1,6-bisphosphate derivatives of D-tagatose, D-fructose, D-sorbose, and D-psicose. LacD.1 and LacD.2 are two closely-related Class I TBP aldolases in Streptococcus pyogenes. Here we have determined the crystal structures of S. aureus LacD and S. pyogenes LacD.1. Monomers of both enzymes are folded into a (β/α)(8) barrel and two monomers associate tightly to form a dimer in the crystals. The structures suggest that the residues E189 and S300 of rabbit muscle Class I fructose-1,6-bisphosphate (FBP) aldolase are important for substrate specificity. When we mutated the corresponding residues of S. aureus LacD, the mutants (L165E, L275S, and L165E/L275S) showed enhanced substrate specificity toward FBP.

PubMed: 21192932
DOI: 10.1016/j.febslet.2010.12.038

Experimental method

X-RAY DIFFRACTION (2.5 Å)