3myo

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

spinqualitylabelsall models 3myo, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3myo is a 2 chain structure with sequence from Streptococcus pyogenes serotype M1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LACD1_STRP1 Publication Abstract from PubMed 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 (beta/alpha)(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. STRUCTURED SUMMARY: lacDbinds to lacD by X-ray crystallography(View interaction) lacD1binds to lacD1 by X-ray crystallography(View interaction). Crystal structures of LacD from Staphylococcus aureus and LacD.1 from Streptococcus pyogenes: Insights into substrate specificity and virulence gene regulation.,Lee SJ, Kim HS, Kim do J, Yoon HJ, Kim KH, Yoon JY, Suh SW FEBS Lett. 2011 Jan 21;585(2):307-12. Epub 2010 Dec 28. PMID:21192932 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aldolase 3D structures

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