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Crystal Structure of the Class IV Adenylyl Cyclase From Yersinia Pestis

Published

Author(s)

N Smith, Sung Kim, Prasad T. Reddy, David T. Gallagher

Abstract

ABSTRACT: The crystal structure of the class IV adenylyl cyclase from Yersinia pestis is reported at 1.9 resolution. The class IV fold is distinct from the previously described folds for class II and class III ACs. The dimeric Yp AC-IV folds into an antiparallel 8-stranded barrel whose connectivity has been seen in only 3 previous structures: yeast RNA triphosphatase and two proteins of unknown function from Pyrococcus furiosus and Vibrio parahaemolyticus. These 3 structures, and a larger group of known sequences, span the 3 kingdoms of life and delineate an ancient family of phosphonucletide processing enzymes. A group of conserved ionic residues inside the barrel forms the likely binding sites for substrate and divalent cations. Unlike AC-II and AC-III active sites that utilize a DxD motif for cation binding, the AC-IV active site contains only one conserved Asp and instead features an ExE motif. Previous predictions for the overall fold and active site structure in this CYTH family are found to be mostly correct.
Citation
ACTA Crystallographica
Volume
62
Issue
Part 3

Keywords

antiparallel 8-stranded barrel, cyclic AMP, evolution, phosphonucleotide, x-ray diffraction

Citation

Smith, N. , Kim, S. , Reddy, P. and Gallagher, D. (2006), Crystal Structure of the Class IV Adenylyl Cyclase From Yersinia Pestis, ACTA Crystallographica (Accessed February 27, 2024)
Created March 1, 2006, Updated February 19, 2017