The crystal structure of the AF2331 protein from Archaeoglobus fulgidus DSM 4304 forms an unusual interdigitated dimer with a new type of α + β fold

Protein Science

Volumn 18, Issue 11, 2009, Pages 2410-2419

  Wang, Shuren ^a,b   Kirillova, Olga ^a,b   Chruszcz, Maksymilian ^a,b   Gront, Dominik ^a,b   Zimmerman, Matthew D ^a,b   Cymborowski, Marcin T ^a,b   Shumilin, Igor A ^a,b   Skarina, Tatiana ^b,c   Gorodichtchenskaia, Elena ^b,c   Savchenko, Alexei ^b,c   Edwards, Aled M ^b,c   Minor, Wladek ^a,b  

^a UNIVERSITY OF VIRGINIA   (United States)

^b Midwest Center for Structural Genomics   (United States)

^c UNIVERSITY OF TORONTO   (Canada)

Author keywords

Archaeoglobus fulgidus; Dimerization; Homo oligomers; New type of + fold; Orphan protein

Indexed keywords

BASIC PROTEIN; DIMER;

ARCHAEOGLOBUS FULGIDUS; ARTICLE; BETA SHEET; CONTROLLED STUDY; CRYSTAL STRUCTURE; HYPOTHESIS; IN VIVO STUDY; NONHUMAN; OPERON; PRIORITY JOURNAL; PROTEIN FOLDING;

ARCHAEAL PROTEINS; ARCHAEOGLOBUS FULGIDUS; COMPUTATIONAL BIOLOGY; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY;

ARCHAEOGLOBUS FULGIDUS; ARCHAEOGLOBUS FULGIDUS DSM 4304;

EID: 70350519377     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.251     Document Type: Article

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