Sandbox Reserved 434

This Sandbox is Reserved from January 19, 2016, through August 31, 2016 for use for Proteopedia Team Projects by the class Chemistry 423 Biochemistry for Chemists taught by Lynmarie K Thompson at University of Massachusetts Amherst, USA. This reservation includes Sandbox Reserved 425 through Sandbox Reserved 439.

Pantetheinase (4CYG)Pantetheinase (4CYG)[1]

by [Luke Schnitzler, Patrick Tonne, Owen O'Connor, Tyler Russell, Nicholas Sant]

Student Projects for UMass Chemistry 423 Spring 2016 <StructureSection load='4CYG' size='350' side='right' caption='caption for Molecular Playground (PDB entry 4CYG)' scene=>

IntroductionIntroduction

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 StructureOverall 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 InteractionsBinding 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 FeaturesAdditional Features

- Issues when protein loses function - relation to cysteamine (what happens when cysteamine production goes down?) - Methods of testing

Quiz Question 1Quiz Question 1

- Additional research needed to formulate question (may potentially pertain to structure-substrate interaction)

See AlsoSee Also

• 1h1t
• 1mop
• 1esm

CreditsCredits

Introduction - Patrick Tonne

Overall Structure - Luke Schnitzler

Drug Binding Site - Owen O'Connor

Additional Features - Nick Saint

Quiz Question 1 - Tyler Russell