Ontology highlight
ABSTRACT:
SUBMITTER: Das D
PROVIDER: S-EPMC2954202 | biostudies-literature | 2010 Oct
REPOSITORIES: biostudies-literature
Das Debanu D Grishin Nick V NV Kumar Abhinav A Carlton Dennis D Bakolitsa Constantina C Miller Mitchell D MD Abdubek Polat P Astakhova Tamara T Axelrod Herbert L HL Burra Prasad P Chen Connie C Chiu Hsiu Ju HJ Chiu Michelle M Clayton Thomas T Deller Marc C MC Duan Lian L Ellrott Kyle K Ernst Dustin D Farr Carol L CL Feuerhelm Julie J Grzechnik Anna A Grzechnik Slawomir K SK Grant Joanna C JC Han Gye Won GW Jaroszewski Lukasz L Jin Kevin K KK Johnson Hope A HA Klock Heath E HE Knuth Mark W MW Kozbial Piotr P Krishna S Sri SS Marciano David D McMullan Daniel D Morse Andrew T AT Nigoghossian Edward E Nopakun Amanda A Okach Linda L Oommachen Silvya S Paulsen Jessica J Puckett Christina C Reyes Ron R Rife Christopher L CL Sefcovic Natasha N Tien Henry J HJ Trame Christine B CB van den Bedem Henry H Weekes Dana D Wooten Tiffany T Xu Qingping Q Hodgson Keith O KO Wooley John J Elsliger Marc André MA Deacon Ashley M AM Godzik Adam A Lesley Scott A SA Wilson Ian A IA
Acta crystallographica. Section F, Structural biology and crystallization communications 20091027 Pt 10
Proteins with the DUF2063 domain constitute a new Pfam family, PF09836. The crystal structure of a member of this family, NGO1945 from Neisseria gonorrhoeae, has been determined and reveals that the N-terminal DUF2063 domain is likely to be a DNA-binding domain. In conjunction with the rest of the protein, NGO1945 is likely to be involved in transcriptional regulation, which is consistent with genomic neighborhood analysis. Of the 216 currently known proteins that contain a DUF2063 domain, the m ...[more]