The gene ATP7B has three different types of protein domains. E1-E2_ATPase, Heavy
ID: 174329 • Letter: T
Question
The gene ATP7B has three different types of protein domains. E1-E2_ATPase, Heavy metal Associated domain(HMA) and Soluble P-type ATPase. Describe the domain structures of all three types(ex. Beta sheets, alpha helices) and how their structure helps and relates to the function of the protein which is copper transport. The gene ATP7B has three different types of protein domains. E1-E2_ATPase, Heavy metal Associated domain(HMA) and Soluble P-type ATPase. Describe the domain structures of all three types(ex. Beta sheets, alpha helices) and how their structure helps and relates to the function of the protein which is copper transport.Explanation / Answer
Answer:
The gene ATP7B is belongs to P-type cation transport ATPase and it is going to code for three different types of protein domains. E1-E2_ATPase, Heavy metal Associated domain(HMA) and Soluble P-type ATPase. The E1-E2 ATPases also referred as P-type ATPase and the structure is composed of approximately 10 transmmebrane helical domains in its secondary structure together to form conserved structure (ex. In case of sarcoplasmic reticulum SERCA2+, we can find P- domain, A d-main etc with Beta sheets, alpha helices of P-type ATPases, for calcium trasport) that helps copper transport due to presence "copper binding sites". This alpha-helical strcture of P-type ATPase binding to "copper" is profoundly promoted along with heavy-metal-associated domain (HMA). HMA domain is composed of 2 conserved cysteine residues to bind to “copper metal transport i.e. hepatic efflux of copper into bile”. The structure of HMA (Menke's copper transporting ATPase) is going to enable a hinge domain of 4 antiparalel beta sheets & 2 alpha sheets with Ptype- ATPase consensus. These domains have 2 copper binding sites to transport copper into the bile
Related Questions
drjack9650@gmail.com
Navigate
Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.