Crystallization of the class IV adenylyl cyclase from Yersinia pestis

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
N Natasha SmithD Travis Gallagher

Abstract

The class IV adenylyl cyclase from Yersinia pestis has been cloned and crystallized in both a triclinic and an orthorhombic form. An amino-terminal His-tagged construct, from which the tag was removed by thrombin, crystallized in a triclinic form diffracting to 1.9 A, with one dimer per asymmetric unit and unit-cell parameters a = 33.5, b = 35.5, c = 71.8 A, alpha = 88.7, beta = 82.5, gamma = 65.5 degrees. Several mutants of this construct crystallized but diffracted poorly. A non-His-tagged native construct (179 amino acids, MW = 20.5 kDa) was purified by conventional chromatography and crystallized in space group P2(1)2(1)2(1). These crystals have unit-cell parameters a = 56.8, b = 118.6, c = 144.5 A, diffract to 3 A and probably have two dimers per asymmetric unit and VM = 3.0 A3 Da(-1). Both crystal forms appear to require pH below 5, complicating attempts to incorporate nucleotide ligands into the structure. The native construct has been produced as a selenomethionine derivative and crystallized for phasing and structure determination.

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Citations

Nov 15, 2011·Nature Reviews. Microbiology·Kathleen A McDonough, Ana Rodriguez
Aug 16, 2011·The Journal of Biological Chemistry·David DelvauxLucien Bettendorff
Sep 12, 2013·The FEBS Journal·Lucien Bettendorff, Pierre Wins
Nov 26, 2010·Journal of Molecular Biology·D Travis GallagherPrasad T Reddy
Aug 15, 2006·Journal of Molecular Biology·D Travis GallagherPrasad T Reddy
Apr 1, 2014·Microbiology Spectrum·Gwendowlyn S Knapp, Kathleen A McDonough

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