1y10
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(New page: 200px<br /><applet load="1y10" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y10, resolution 2.30Å" /> '''Mycobacterial adenyl...)
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Revision as of 04:21, 21 November 2007
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Mycobacterial adenylyl cyclase Rv1264, holoenzyme, inhibited state
Overview
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 degrees to form two catalytic sites at their interface. Two alpha, 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.
About this Structure
1Y10 is a Single protein structure of sequence from Mycobacterium tuberculosis with CA and 1PE as ligands. Active as Adenylate cyclase, with EC number 4.6.1.1 Full crystallographic information is available from OCA.
Reference
The structure of a pH-sensing mycobacterial adenylyl cyclase holoenzyme., Tews I, Findeisen F, Sinning I, Schultz A, Schultz JE, Linder JU, Science. 2005 May 13;308(5724):1020-3. PMID:15890882
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