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Structural impact of TM domain mutations on mycobacterial adenylyl cyclase Rv1625c (LiP-MS)

ABSTRACT: LiP-MS was used to assess the structural impact of transmembrane domain mutations on the overall conformation of the mycobacterial cycase Rv1625c.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Escherichia Coli Mycobacterium Tuberculosis Sumu001

TISSUE(S): Cell Culture

SUBMITTER: Dina Schuster

LAB HEAD: Volodymyr Korkhov

PROVIDER: PXD033826 | Pride | 2022-08-19

REPOSITORIES: Pride

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Structure of <i>Mycobacterium tuberculosis</i> Cya, an evolutionary ancestor of the mammalian membrane adenylyl cyclases.

Mehta Ved V Khanppnavar Basavraj B Schuster Dina D Kantarci Ilayda I Vercellino Irene I Kosturanova Angela A Iype Tarun T Stefanic Sasa S Picotti Paola P Korkhov Volodymyr M VM

eLife 20220818

<i>Mycobacterium tuberculosis</i> 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 facilita ...[more]

PMID: 35980026

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