7vcm

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crystal structure of GINKO1

Structural highlights

7vcm is a 2 chain structure with sequence from Aequorea victoria and Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Ligands:CRO, K
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KBP_ECOLI Highly specific potassium binding protein that is required for normal growth in the presence of high levels of external K(+). May act as a sensor of cytoplasmic K(+) concentration. Binds a single K(+) ion, which induces a large conformational change. Can also bind the larger alkali metal ions Rb(+) and Cs(+), and NH(4)(+) (PubMed:27112601). May be involved in the regulation of peptidoglycan cross-linking (PubMed:25422305).[1] [2] GFP_AEQVI Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.

Publication Abstract from PubMed

Potassium ion (K+) plays a critical role as an essential electrolyte in all biological systems. Genetically-encoded fluorescent K+ biosensors are promising tools to further improve our understanding of K+-dependent processes under normal and pathological conditions. Here, we report the crystal structure of a previously reported genetically-encoded fluorescent K+ biosensor, GINKO1, in the K+-bound state. Using structure-guided optimization and directed evolution, we have engineered an improved K+ biosensor, designated GINKO2, with higher sensitivity and specificity. We have demonstrated the utility of GINKO2 for in vivo detection and imaging of K+ dynamics in multiple model organisms, including bacteria, plants, and mice.

A sensitive and specific genetically-encoded potassium ion biosensor for in vivo applications across the tree of life.,Wu SY, Wen Y, Serre NBC, Laursen CCH, Dietz AG, Taylor BR, Drobizhev M, Molina RS, Aggarwal A, Rancic V, Becker M, Ballanyi K, Podgorski K, Hirase H, Nedergaard M, Fendrych M, Lemieux MJ, Eberl DF, Kay AR, Campbell RE, Shen Y PLoS Biol. 2022 Sep 6;20(9):e3001772. doi: 10.1371/journal.pbio.3001772. , eCollection 2022 Sep. PMID:36067248[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
4 reviews cite this structure
Torres-Ocampo et al. (2023)
No citations found

See Also

References

  1. Bernal-Cabas M, Ayala JA, Raivio TL. The Cpx envelope stress response modifies peptidoglycan cross-linking via the L,D-transpeptidase LdtD and the novel protein YgaU. J Bacteriol. 2015 Feb;197(3):603-14. doi: 10.1128/JB.02449-14. Epub 2014 Nov 24. PMID:25422305 doi:http://dx.doi.org/10.1128/JB.02449-14
  2. Ashraf KU, Josts I, Mosbahi K, Kelly SM, Byron O, Smith BO, Walker D. The Potassium Binding Protein Kbp Is a Cytoplasmic Potassium Sensor. Structure. 2016 May 3;24(5):741-9. doi: 10.1016/j.str.2016.03.017. Epub 2016 Apr , 21. PMID:27112601 doi:http://dx.doi.org/10.1016/j.str.2016.03.017
  3. Wu SY, Wen Y, Serre NBC, Laursen CCH, Dietz AG, Taylor BR, Drobizhev M, Molina RS, Aggarwal A, Rancic V, Becker M, Ballanyi K, Podgorski K, Hirase H, Nedergaard M, Fendrych M, Lemieux MJ, Eberl DF, Kay AR, Campbell RE, Shen Y. A sensitive and specific genetically-encoded potassium ion biosensor for in vivo applications across the tree of life. PLoS Biol. 2022 Sep 6;20(9):e3001772. PMID:36067248 doi:10.1371/journal.pbio.3001772

Contents


PDB ID 7vcm

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