The work is carefully performed, with insights from three dimensional structures used to understand the structural basis for how/why the presumed MVAPP decarboxylase has an altered substrate specificity that allows the MVAP decarboxylase activity.
This prompted us to utilize the information provided by the transition state structure of MnmE to understand the structural basis for the role of potassium in GTP hydrolysis.
To understand the structural basis for this, we determined crystal structures of a replicative DNA polymerase from bacteriophage T7 in complex with nucleotide substrates and a DNA template containing a cis-syn cyclobutane pyrimidine dimer (CPD).
To understand the structural basis for HMW1 glycosylation, we have pursued structure and function studies of HMW1C.
To further understand the structural basis for selectivity, we determined the crystal structure of CpOGA in complex with GlcNAcstatin D. These data show that GlcNAcstatin D binds deep into the active site of CpOGA, with the sugar moiety adopting a E conformation, and assuming the same conformation as observed for the GlcNAcstatin C complex [ 41].
In order to understand the structural basis underlying this specificity, we determined crystal structures of three mutant APPBP1-UBA3-NEDD8 complexes: "wild-type-opposite" [UBA3Arg190Ala-NEDD8Ala72.85, 2.85 Å resolution]; "ubiquitinized" [UBA3Arg190Gln-NEDD8Ala72Arg, 3.05 Å resolution]; and "ubiquitinized-opposite" [UBA3Arg190 (wt -NEDD8Ala72Gln, 2.90 Å resolution].
In order to better understand the structural basis of ubiquitin UIM recognition, we have characterized changes in the structure and dynamics of ubiquitin upon binding of a UIM domain from the yeast Vps27 protein.
To understand the structural basis of AcrR regulation, we have determined the crystal structure of AcrR to 2.55-Å resolution, revealing a dimeric two-domain molecule with an entirely helical architecture similar to members of the TetR family of transcriptional regulators.
To understand the structural basis of CmeR regulation, we have determined the crystal structure of CmeR to 2.2 Å resolution, revealing a dimeric two-domain molecule with an entirely helical architecture similar to members of the TetR family of transcriptional regulators.
To understand the structural basis of these contrasting characteristics, we determined the crystal structures of the tengpinΔ31 and tengpinΔ51 constructs.
