Comparison of the NMR solution structure with the X-ray crystal structure of the activation domain from procarboxypeptidase B |
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Authors: | M. Billeter J. Vendrell G. Wider F. X. Avilés M. Coll A. Guasch R. Huber K. Wüthrich |
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Affiliation: | (1) Eidgenössische Technische Hochschule-Hönggerberg, Institut für Molekularbiologie und Biophysik, CH-8093 Zürich, Switzerland;(2) Departament de Bioquimica i Biologia Molecular, Faculta de Ciències, Universital Autònoma de Barcelona, E-08193 Bellaierra (Barcelona), Spain;(3) Max-Planck-Institut für Biochemie, D-8033 Martinsried bei München, Germany;(4) Unitat de Quimica Macromolecular (CSIC) ETS, Enginyers Industrials, Diagonal 647, E-08028 Barcelona, Spain |
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Abstract: | Summary 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 Å. 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. |
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Keywords: | Protein structure NMR solution structure X-ray crystal structure Procarboxypeptidase B Activation domain B |
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