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TitleAllosteric regulation of nitrate transporter NRT via the signaling protein PII.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 121, Issue 11, Page e2318320121, Year 2024
Publish dateMar 12, 2024
AuthorsBo Li / Xiao-Qian Wang / Qin-Yao Li / Da Xu / Jing Li / Wen-Tao Hou / Yuxing Chen / Yong-Liang Jiang / Cong-Zhao Zhou /
PubMed AbstractCoordinated carbon and nitrogen metabolism is crucial for bacteria living in the fluctuating environments. Intracellular carbon and nitrogen homeostasis is maintained by a sophisticated network, in ...Coordinated carbon and nitrogen metabolism is crucial for bacteria living in the fluctuating environments. Intracellular carbon and nitrogen homeostasis is maintained by a sophisticated network, in which the widespread signaling protein PII acts as a major regulatory hub. In cyanobacteria, PII was proposed to regulate the nitrate uptake by an ABC (ATP-binding cassette)-type nitrate transporter NrtABCD, in which the nucleotide-binding domain of NrtC is fused with a C-terminal regulatory domain (CRD). Here, we solved three cryoelectron microscopy structures of NrtBCD, bound to nitrate, ATP, and PII, respectively. Structural and biochemical analyses enable us to identify the key residues that form a hydrophobic and a hydrophilic cavity along the substrate translocation channel. The core structure of PII, but not the canonical T-loop, binds to NrtC and stabilizes the CRD, making it visible in the complex structure, narrows the substrate translocation channel in NrtB, and ultimately locks NrtBCD at an inhibited inward-facing conformation. Based on these results and previous reports, we propose a putative transport cycle driven by NrtABCD, which is allosterically inhibited by PII in response to the cellular level of 2-oxoglutarate. Our findings provide a distinct regulatory mechanism of ABC transporter via asymmetrically binding to a signaling protein.
External linksProc Natl Acad Sci U S A / PubMed:38457518 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.54 Å
Structure data

37375

8w9m

EMDB-37375: Allosteric regulation of nitrate transporter NRT via the signalling protein PII
PDB-8w9m: Cryo-EM structure of the cyanobacterial nitrate transporter NrtBCD in complex with ATP
Method: EM (single particle) / Resolution: 3.1 Å

37644

8wm7

EMDB-37644, PDB-8wm7:
Cryo-EM structure of cyanobacterial nitrate/nitrite transporter NrtBCD in complex with signalling protein PII
Method: EM (single particle) / Resolution: 3.53 Å

37645

8wm8

EMDB-37645, PDB-8wm8:
Cryo-EM structure of cyanobacterial nitrate/nitrite transporter NrtBCD in complex with nitrate
Method: EM (single particle) / Resolution: 3.54 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-NO3:
NITRATE ION / Nitrate

Source
  • nostoc sp. pcc 7120 = fachb-418 (bacteria)
  • nostoc sp. (bacteria)
KeywordsMEMBRANE PROTEIN / ATP-dependent transporter / ABC transporter / nitrate/nitrite transporter

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