1s7o
From Proteopedia
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, resolution 2.31Å | |||||||
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Gene: | SPY1201, SPYM3_0842, SPS1042, SPYM18_1152 (Streptococcus pyogenes) | ||||||
Domains: | PRK00118 | ||||||
Resources: | FirstGlance, OCA, PDBsum, JenaLib, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of putative DNA binding protein SP_1288 from Streptococcus pygenes
Overview
The crystal structure of the putative DNA-binding protein SP_1288 (gi/15675166, also listed as gi/28895954) from Streptococcus pyogenes has been determined by X-ray crystallography to a resolution of 2.3 A using anomalous diffraction data at the Se peak wavelength. SP_1288 belongs to a family of proteins whose cellular function is associated with the signal recognition particle; no structural information has been available until now about the members of the family. Crystallographic analysis revealed that the overall fold of SP_1288 consists exclusively of alpha-helices and that 75% of the structure has good similarity to domain 4 of the sigma subunit of RNA polymerase. This suggests its possible involvement in the biochemical function of transcription initiation, which includes interaction with DNA.
About this Structure
1S7O is a Single protein structure of sequence from Streptococcus pyogenes. Full crystallographic information is available from OCA.
Reference
Structure of the putative DNA-binding protein SP_1288 from Streptococcus pyogenes., Oganesyan V, Pufan R, DeGiovanni A, Yokota H, Kim R, Kim SH, Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1266-71. Epub 2004, Jun 22. PMID:15213388
Page seeded by OCA on Wed Mar 26 06:04:23 2008
Categories: Single protein | Streptococcus pyogenes | BSGC, Berkeley Structural Genomics Center. | DeGiovanni, A. | Kim, R. | Kim, S H. | Oganesyan, V. | Pufan, R. | Yokota, H. | Berkeley structural genomics center | Bsgc | Protein structure initiative | Psi | Putative dna binding protein | Rna polymerase sigma factor | Signal recognition particle | Structural genomic | Structure funded by nih | Upf0122 | X-rat crystallography