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	== Structural highlights ==		== Structural highlights ==
-	This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.	+	The two domains of hexokinase are connected by a single alpha-helix. This creates a cleft region which acts as the active site for the enzyme.

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Revision as of 14:34, 4 November 2022

This Sandbox is Reserved from August 30, 2022 through May 31, 2023 for use in the course Biochemistry I taught by Kimberly Lane at the Radford University, Radford, VA, USA. This reservation includes Sandbox Reserved 1730 through Sandbox Reserved 1749.

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Contents 1 Structure 2 Function 3 Disease 4 Relevance 5 Structural highlights 6 References

Structure

spinqualitylabelsall models Insert caption here Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Primary Structure: ~461 amino acids

Secondary Structure: 12 alpha helicies, 12 beta strands

Tertiary Structure: N-Terminal Regulatory Domain, C-Terminal Catalytic Domain

Quaternary Structure: Forms a homodimer

Function

Glucose binds to hexokinase, which is then attacked by ATP. The terminal phosphate group on the ATP binds to the glucose, creating two products: glucose-6-phosphate, and ADP. Hexokinase serves as a catalyst for this reaction.

Disease

Relevance

Structural highlights

The two domains of hexokinase are connected by a single alpha-helix. This creates a cleft region which acts as the active site for the enzyme.

References

1. D. J. Roberts, S. Miyamoto. Hexokinase II integrates energy metabolism and cellular protection: Akting on mitochondria and TORCing to autophagy. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4291497/ (Accessed 10/21/2022).

2. Anne M. Mulichuk, John E. Wilson, Kaillathe Padmanabhan, Michael Garavito. The structure of mammalian hexokinase-1. https://www.nature.com/articles/nsb0798_555. (Accessed 10/21/2022).

3. Valerie P. Tan, Shigeki Miyamoto. HK2/hexokinase-II integrates glycolysis and autophagy to confer cellular protection. https://pubmed.ncbi.nlm.nih.gov/26075878/. (Accessed 10/21/2022).

4. M. Magnani, M. Bianchi, A. Casabianca, V. Stocchi, A. Daniele, F. Altruda, M. Ferrone, L. Silengo. A recombinant human 'mini'-hexokinase is catalytically active and regulated by hexose 6-phosphates. https://pubmed.ncbi.nlm.nih.gov/1637300/. (Accessed 10/21/2022).

5. A. E. Aleshin, C. Zeng, G. P. Bourenkov, H. D. Bartunik, H. J. Fromm, R. B. Honzatko. The mechanism of regulation of hexokinase: new insights from the crystal structure of recombinant human brain hexokinase complexed with glucose and glucose-6-phosphate. https://pubmed.ncbi.nlm.nih.gov/9493266/. (Accessed 10/21/2022).

6. Richard Southworth, Katherine A. B. Davey, Alice Warley, Pamela B. Garlick. A reevaluation of the roles of hexokinase I and II in the heart. https://journals.physiology.org/doi/full/10.1152/ajpheart.00664.2006. (Accessed 10/21/2022)

7. Èric Claeyssen, Jean Rivoal. Isozymes of plant hexokinase: Occurrence, properties and functions. https://www.sciencedirect.com/science/article/abs/pii/S0031942206007606. (Accessed 10/21/2022)