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The structure of vanin 1: a key enzyme linking metabolic disease and inflammation.
MedLine Citation:
PMID:  25478849     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Although part of the coenzyme A pathway, vanin 1 (also known as pantetheinase) sits on the cell surface of many cell types as an ectoenzyme, catalyzing the breakdown of pantetheine to pantothenic acid (vitamin B5) and cysteamine, a strong reducing agent. Vanin 1 was initially discovered as a protein involved in the homing of leukocytes to the thymus. Numerous studies have shown that vanin 1 is involved in inflammation, and more recent studies have shown a key role in metabolic disease. Here, the X-ray crystal structure of human vanin 1 at 2.25 Å resolution is presented, which is the first reported structure from the vanin family, as well as a crystal structure of vanin 1 bound to a specific inhibitor. These structures illuminate how vanin 1 can mediate its biological roles by way of both enzymatic activity and protein-protein interactions. Furthermore, it sheds light on how the enzymatic activity is regulated by a novel allosteric mechanism at a domain interface.
Authors:
Ykelien L Boersma; Janet Newman; Timothy E Adams; Nathan Cowieson; Guy Krippner; Kiymet Bozaoglu; Thomas S Peat
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2014-11-28
Journal Detail:
Title:  Acta crystallographica. Section D, Biological crystallography     Volume:  70     ISSN:  1399-0047     ISO Abbreviation:  Acta Crystallogr. D Biol. Crystallogr.     Publication Date:  2014 Dec 
Date Detail:
Created Date:  2014-12-5     Completed Date:  -     Revised Date:  2014-12-6    
Medline Journal Info:
Nlm Unique ID:  9305878     Medline TA:  Acta Crystallogr D Biol Crystallogr     Country:  -    
Other Details:
Languages:  ENG     Pagination:  3320-3329     Citation Subset:  -    
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