Results 5

STRUCTURE

Quality of YlqF protein model and overall structure

The asymmetric unit of Bacillus subtilis YlqF protein consists of a polymer containing 282 amino acids (Figure 1). The protein has been refined at 2 angstroms to a crystallographic R factor of 21.6% and free R factor of 25%. Table 1 summarizes the refinement statistics including protein quality parameters. MolProbity Ramachandran analysis of YlqF in shows that 96.5% of all residues lie in the favoured regions and 98.8% of all residues lie in the allowed regions.

Table 1. Crystal parameters and refinement statistics

Parameters

Resolution[Å] 2.00

R factor, % 21.6

Free R factor, % 25.0

Space Group P 21 21 21

Unit Cell	Length[Å] Angles [°]	a alpha	36.75 90.00	b beta	68.57 90.00	c gamma	105.57 90.00

  1 - MTIQWFPGHM AKARREVTEK LKLIDIVYEL VDARIPMSSR NPMIEDILKN KPRIMLLNKA
 61 - DKADAAVTQQ WKEHFENQGI RSLSINSVNG QGLNQIVPAS KEILQEKFDR MRAKGVKPRA
121 - IRALIIGIPN VGKSTLINRL AKKNIAKTGD RPGITTSQQW VKVGKELELL DTPGILWPKF
181 - EDELVGLRLA VTGAIKDSII NLQDVAVFGL RFLEEHYPER LKERYGLDEI PEDIAELFDA
241 - IGEKRGCLMS GGLINYDKTT EVIIRDIRTE KFGRLSFEQP TM

Figure 1. Amino acid sequence of YlqF

The secondary structure of YlqF mainly contains 50% helical (13 helices; 142 residues) and 10% beta sheet (6 strands; 31 residues)(see Figure 2). YlqF protein consists of two domains. One domain contains Rossmann fold with α/β class. This domain possesses 1-177 residues, and forms a 3-layer sandwich structure. The other one is referred to as a conserved hypothetical protein with mainly α class. This possesses 178-282 residues, and forms a orthogonal bundle structure. YlqF is also classified as a signalling protein. The molecular weight of the protein is 31986 Da.

= pi helix, = 310 helix, = extended strand, = turn, = alpha helix, Greyed out residues have no structural information

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