1Y10
Mycobacterial adenylyl cyclase Rv1264, holoenzyme, inhibited state
Summary for 1Y10
| Entry DOI | 10.2210/pdb1y10/pdb |
| Related | 1Y11 |
| Descriptor | Hypothetical protein Rv1264/MT1302, CALCIUM ION, PENTAETHYLENE GLYCOL, ... (4 entities in total) |
| Functional Keywords | adenylyl cyclase fold, lyase |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 4 |
| Total formula weight | 175016.43 |
| Authors | Tews, I.,Findeisen, F.,Sinning, I.,Schultz, A.,Schultz, J.E.,Linder, J.U. (deposition date: 2004-11-16, release date: 2005-05-24, Last modification date: 2024-04-03) |
| Primary citation | Tews, I.,Findeisen, F.,Sinning, I.,Schultz, A.,Schultz, J.E.,Linder, J.U. The structure of a pH-sensing mycobacterial adenylyl cyclase holoenzyme Science, 308:1020-1023, 2005 Cited by PubMed 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 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. PubMed: 15890882DOI: 10.1126/science.1107642 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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