3MYP
Crystal structure of tagatose-1,6-bisphosphate aldolase from Staphylococcus aureus
Summary for 3MYP
| Entry DOI | 10.2210/pdb3myp/pdb |
| Related | 3MYO |
| Descriptor | Tagatose 1,6-diphosphate aldolase (2 entities in total) |
| Functional Keywords | beta-alpha-barrel, lyase |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 4 |
| Total formula weight | 151779.92 |
| 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: 2024-10-16) |
| 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 Cited by 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: 21192932DOI: 10.1016/j.febslet.2010.12.038 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.99 Å) |
Structure validation
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