Introduction
The two protein subunits possess dense regions of
Main points:
- introduce general characteristics of protein (location within cell, substrate activity, relation to cysteamine)
- A small paragraph on its discovery
- The broad impact of the protein (what happens if it loses function?)
Overall Structure
- 506 total residues, 87 missing
- Two chains, each with many alpha helices and beta sheets
-
43 missing residues: 8-20, 484-513
- Chain B
44 missing residues: 8-20, 484-513
Ligands and non-standard residues
- 2 RRV
- 2 PEG
- 8 NAG
Binding Interactions
Vanin-1 binds with 3 unique ligands including PEG (DI(HYDROXYETHYL)ETHER), NAG (N-ACETYL-D-GLUCOSAMINE) and RRV ((2R)-2,4-dihydroxy-N-[(3S)-3-hydroxy-4-phenylbutyl]-3,3-dimethylbutanamide). NAG and RRV both bind in the alpha helixes and beta strands but PEG only binds to the beta strands.
Vanin 1 is a key protein that is involved in the breakdown of pantetheine to panthothenic acid and cysteamine. These proteins are associated with many metabolic diseases like type 2 diabetes. Understanding the binding interaction would give insight into treating these diseases more effectively. Vanin 1 has three catalytic residues (Glu79, Lys178 and Cys211) that represents the active site of the enzyme.The active site is located in the center of the enzyme in between the two sub-units. It was discovered that Glu79 and Lys178 were responsible for orienting and activating Cys211 to catalyze the reaction.
Additional Features
- Issues when protein loses function
- relation to cysteamine (what happens when cysteamine production goes down?)
- Methods of testing
Quiz Question 1
- Additional research needed to formulate question (may potentially pertain to structure-substrate interaction)
See Also
Credits
Introduction - Patrick Tonne
Overall Structure - Luke Schnitzler
Drug Binding Site - Owen O'Connor
Additional Features - Nick Saint
Quiz Question 1 - Tyler Russell
References
- ↑ Boersma YL, Newman J, Adams TE, Cowieson N, Krippner G, Bozaoglu K, Peat TS. The structure of vanin 1: a key enzyme linking metabolic disease and inflammation. Acta Crystallogr D Biol Crystallogr. 2014 Dec 1;70(Pt 12):3320-9. doi:, 10.1107/S1399004714022767. Epub 2014 Nov 28. PMID:25478849 doi:http://dx.doi.org/10.1107/S1399004714022767
