7YZK
Structure of Mycobacterium tuberculosis adenylyl cyclase Rv1625c / Cya
Summary for 7YZK
| Entry DOI | 10.2210/pdb7yzk/pdb |
| EMDB information | 14389 |
| Descriptor | Adenylate cyclase, Nanobody Nb4, 3'-O-(N-METHYLANTHRANILOYL)-GUANOSINE-5'-TRIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | adenylyl cyclase, membrane protein, cyclic adenosine monophosphate, signal transduction, nanobody |
| Biological source | Mycobacterium tuberculosis More |
| Total number of polymer chains | 4 |
| Total formula weight | 129847.99 |
| Authors | Mehta, V.,Khanppnavar, B.,Korkhov, V.M. (deposition date: 2022-02-20, release date: 2022-08-31, Last modification date: 2024-11-13) |
| Primary citation | Mehta, V.,Khanppnavar, B.,Schuster, D.,Kantarci, I.,Vercellino, I.,Kosturanova, A.,Iype, T.,Stefanic, S.,Picotti, P.,Korkhov, V.M. Structure of Mycobacterium tuberculosis Cya, an evolutionary ancestor of the mammalian membrane adenylyl cyclases. Elife, 11:-, 2022 Cited by PubMed Abstract: adenylyl cyclase (AC) Rv1625c/Cya is an evolutionary ancestor of the mammalian membrane ACs and a model system for studies of their structure and function. Although the vital role of ACs in cellular signalling is well established, the function of their transmembrane (TM) regions remains unknown. Here, we describe the cryo-EM structure of Cya bound to a stabilizing nanobody at 3.6 Å resolution. The TM helices 1-5 form a structurally conserved domain that facilitates the assembly of the helical and catalytic domains. The TM region contains discrete pockets accessible from the extracellular and cytosolic side of the membrane. Neutralization of the negatively charged extracellular pocket Ex1 destabilizes the cytosolic helical domain and reduces the catalytic activity of the enzyme. The TM domain acts as a functional component of Cya, guiding the assembly of the catalytic domain and providing the means for direct regulation of catalytic activity in response to extracellular ligands. PubMed: 35980026DOI: 10.7554/eLife.77032 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.57 Å) |
Structure validation
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