7yz9 | pdb_00007yz9

Structure of catalytic domain of Rv1625c bound to nanobody NB4

spinqualitylabelsall models 7yz9, resolution 1.97Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7yz9 is a 2 chain structure with sequence from Mycobacterium tuberculosis H37Rv and Vicugna pacos. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.97Å Ligands: GOL, MN, ONM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CYA1_MYCTU Publication Abstract from PubMed Mycobacterium tuberculosis 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 signaling 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 A 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. Structure of Mycobacterium tuberculosis Cya, an evolutionary ancestor of the mammalian membrane adenylyl cyclases.,Mehta V, Khanppnavar B, Schuster D, Kantarci I, Vercellino I, Kosturanova A, Iype T, Stefanic S, Picotti P, Korkhov VM Elife. 2022 Aug 18;11. pii: 77032. doi: 10.7554/eLife.77032. PMID:35980026 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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