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8CI4

Crystal structure of doubly S-methanethiolated rabbit M-type creatine kinase

Summary for 8CI4
Entry DOI10.2210/pdb8ci4/pdb
DescriptorCreatine kinase M-type, CITRATE ANION (3 entities in total)
Functional Keywordsanaerobic metabolism, chemically inactivated, cytosolic protein
Biological sourceOryctolagus cuniculus (rabbit)
Total number of polymer chains1
Total formula weight43840.57
Authors
Joergensen, M.H.,Andersen, D.G.,Andersen, G.R. (deposition date: 2023-02-08, release date: 2023-12-13, Last modification date: 2024-02-21)
Primary citationAndersen, D.G.,Pedersen, A.B.,Jorgensen, M.H.,Montasell, M.C.,Sogaard, A.B.,Chen, G.,Schroeder, A.,Andersen, G.R.,Zelikin, A.N.
Chemical Zymogens and Transmembrane Activation of Transcription in Synthetic Cells.
Adv Mater, 36:e2309385-e2309385, 2024
Cited by
PubMed Abstract: In this work, synthetic cells equipped with an artificial signaling pathway that connects an extracellular trigger event to the activation of intracellular transcription are engineered. Learning from nature, this is done via an engineering of responsive enzymes, such that activation of enzymatic activity can be triggered by an external biochemical stimulus. Reversibly deactivated creatine kinase to achieve triggered production of adenosine triphosphate, and a reversibly deactivated nucleic acid polymerase for on-demand synthesis of RNA are engineered. An extracellular, enzyme-activated production of a diffusible zymogen activator is also designed. The key achievement of this work is that the importance of cellularity is illustrated whereby the separation of biochemical partners is essential to resolve their incompatibility, to enable transcription within the confines of a synthetic cell. The herein designed biochemical pathway and the engineered synthetic cells are arguably primitive compared to their natural counterpart. Nevertheless, the results present a significant step toward the design of synthetic cells with responsive behavior, en route from abiotic to life-like cell mimics.
PubMed: 38009384
DOI: 10.1002/adma.202309385
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.01 Å)
Structure validation

238895

数据于2025-07-16公开中

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