1y10 | pdb_00001y10

Mycobacterial adenylyl cyclase Rv1264, holoenzyme, inhibited state

spinqualitylabelsall models 1y10, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1y10 is a 4 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1PE, CA Related: 1y11 Gene: Rv1264 ("Bacillus tuberculosis" (Zopf 1883) Klein 1884) Activity: Adenylate cyclase, with EC number 4.6.1.1 Resources: FirstGlance, OCA, RCSB, PDBsum Function [Y1264_MYCTU] Catalyzes the formation of the second messenger cAMP. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Adenylyl cyclase

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