The crystal structure of Nep1 reveals an extended SPOUT-class methyltransferase fold and a pre-organized SAM-binding site.

Taylor, Alexander B; Meyer, Britta; Leal, Belinda Z; Kötter, Peter; Schirf, Virgil; Demeler, Borries; Hart, P John; Entian, Karl-Dieter; Wöhnert, Jens

Taylor, Alexander B; Meyer, Britta; Leal, Belinda Z; Kötter, Peter; Schirf, Virgil; Demeler, Borries; Hart, P John; Entian, Karl-Dieter; Wöhnert, Jens.

Affiliation

Taylor AB; Department of Biochemistry, X-ray Crystallography Core Laboratory, The University of Texas Health Science Center San Antonio, San Antonio, TX-78229, USA.

Nucleic Acids Res ; 36(5): 1542-54, 2008 Mar.

Article in En | MEDLINE | ID: mdl-18208838

Subject(s)

Archaeal Proteins/chemistry; Methanococcales/enzymology; Methyltransferases/chemistry; Models, Molecular; S-Adenosylmethionine/chemistry; Amino Acid Sequence; Archaeal Proteins/classification; Archaeal Proteins/metabolism; Binding Sites; Crystallography, X-Ray; Dimerization; Methyltransferases/classification; Methyltransferases/metabolism; Molecular Sequence Data; Protein Folding; Protein Structure, Secondary; RNA/chemistry; RNA, Ribosomal, 18S/metabolism

Fulltext

Add to My VHL

XML

PubMed Links

Search on Google

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: S-Adenosylmethionine / Models, Molecular / Methanococcales / Archaeal Proteins / Methyltransferases Type of study: Prognostic_studies Language: En Journal: Nucleic Acids Res Year: 2008 Document type: Article Affiliation country: United States

Fulltext

Add to My VHL

XML

PubMed Links

Search on Google