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The Structure of a pH-Sensing Mycobacterial Adenylyl Cyclase Holoenzyme

Science  13 May 2005:
Vol. 308, Issue 5724, pp. 1020-1023
DOI: 10.1126/science.1107642

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Abstract

Class III adenylyl cyclases contain catalytic and regulatory domains, yet structural insight into their interactions is missing. We show that the mycobacterial adenylyl cyclase Rv1264 is rendered a pH sensor by its N-terminal domain. In the structure of the inhibited state, catalytic and regulatory domains share a large interface involving catalytic residues. In the structure of the active state, the two catalytic domains rotate by 55° to form two catalytic sites at their interface. Two α helices serve as molecular switches. Mutagenesis is consistent with a regulatory role of the structural transition, and we suggest that the transition is regulated by pH.

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