1G2R

Structure of Cytosolic Protein of Unknown Function Coded by Gene from NUSA/INFB Region, a YlxR Homologue

Summary for 1G2R

• Entry DOI: 10.2210/pdb1g2r/pdb
• Descriptor: HYPOTHETICAL CYTOSOLIC PROTEIN, SULFATE ION (3 entities in total)
• Functional Keywords: hypothetical, nusa-infb operon, streptococcus pneumoniae, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, unknown function
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 1
• Total formula weight: 11833.55

Authors

Osipiuk, J.,Gornicki, P.,Maj, L.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2000-10-20, release date: 2001-08-29, Last modification date: 2024-02-07)

Primary citation

Osipiuk, J.,Gornicki, P.,Maj, L.,Dementieva, I.,Laskowski, R.,Joachimiak, A.
Streptococcus pneumonia YlxR at 1.35 A shows a putative new fold.
Acta Crystallogr.,Sect.D, 57:1747-1751, 2001

PubMed Abstract: The structure of the YlxR protein of unknown function from Streptococcus pneumonia was determined to 1.35 A. YlxR is expressed from the nusA/infB operon in bacteria and belongs to a small protein family (COG2740) that shares a conserved sequence motif GRGA(Y/W). The family shows no significant amino-acid sequence similarity with other proteins. Three-wavelength diffraction MAD data were collected to 1.7 A from orthorhombic crystals using synchrotron radiation and the structure was determined using a semi-automated approach. The YlxR structure resembles a two-layer alpha/beta sandwich with the overall shape of a cylinder and shows no structural homology to proteins of known structure. Structural analysis revealed that the YlxR structure represents a new protein fold that belongs to the alpha-beta plait superfamily. The distribution of the electrostatic surface potential shows a large positively charged patch on one side of the protein, a feature often found in nucleic acid-binding proteins. Three sulfate ions bind to this positively charged surface. Analysis of potential binding sites uncovered several substantial clefts, with the largest spanning 3/4 of the protein. A similar distribution of binding sites and a large sharply bent cleft are observed in RNA-binding proteins that are unrelated in sequence and structure. It is proposed that YlxR is an RNA-binding protein.

PubMed: 11679764
DOI: 10.1107/S0907444901014019

Experimental method

X-RAY DIFFRACTION (1.35 Å)