Comparison of the NMR solution structure with the X-ray crystal structure of the activation domain from procarboxypeptidase B.
The NMR solution structure of the activation domain isolated from porcine procarboxypeptidase B is compared with the X-ray crystal structure of the corresponding segment in the intact proenzyme. For the region of the polypeptide chain that has a well-defined three-dimensional structure in solution, i.e., the backbone atoms of residues 11-76 and 25 amino acid side chains in this segment that form a hydrophobic core in the activation domain, the root-mean-square distance between the two structures is 1.1.A. There are no significant differences in average atom positions between the two structures, but only the NMR structure shows increased structural disorder in three outlying loops located along the same edge of the activation domain. These regions of increased structural disorder in the free domain coincide only partially with the interface to the enzyme domain in the proenzyme.
Billeter
M
M
Institut fur Molekularbiologie und Biophysik, Zurich, Switzerland.
Vendrell
J
J
Wider
G
G
Aviles
F X
FX
Coll
M
M
Guasch
A
A
Huber
R
R
Wuthrich
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D043424:Carboxypeptidase B; D002268:Carboxypeptidases / Q000737:chemistry*; D004792:Enzyme Precursors / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013552:Swine; D014961:X-Ray Diffraction / Q000379:methods
D004792:Enzyme Precursors; D002268:Carboxypeptidases; D043424:Carboxypeptidase B