2g0y

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spinqualitylabelsall models 2g0y, resolution 2.3Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of a Lumenal Pentapeptide Repeat Protein from Cyanothece sp 51142 at 2.3 Angstrom Resolution. Tetragonal Crystal Form

Overview

The genome of the diurnal cyanobacterium Cyanothece sp. PCC 51142 has, recently been sequenced and observed to contain 35 pentapeptide repeat, proteins (PRPs). These proteins, while present throughout the prokaryotic, and eukaryotic kingdoms, are most abundant in cyanobacteria. The sheer, number of PRPs in cyanobacteria coupled with their predicted location in, every cellular compartment argues for important, yet unknown, physiological and biochemical functions. To gain biochemical insights, the, crystal structure for Rfr32, a 167-residue PRP with an N-terminal, 29-residue signal peptide, was determined at 2.1 A resolution. The, structure is dominated by 21 tandem pentapeptide repeats that fold into a, right-handed quadrilateral beta-helix, or Rfr-fold, as observed for the, tandem pentapeptide repeats in the only other PRP structure, the, mycobacterial fluoroquinoline resistance protein MfpA from Mycobacterium, tuberculosis. Sitting on top of the Rfr-fold are two short, antiparallel, alpha-helices, bridged with a disulfide bond, that perhaps prevent, edge-to-edge aggregation at the C terminus. Analysis of the main-chain, (Phi,Psi) dihedral orientations for the pentapeptide repeats in Rfr32 and, MfpA makes it possible to recognize the structural details for the two, distinct types of four-residue turns adopted by the pentapeptide repeats, in the Rfr-fold. These turns, labeled type II and type IV beta-turns, may, be universal motifs that shape the Rfr-fold in all PRPs.

About this Structure

2G0Y is a Protein complex structure of sequences from Cyanothece sp. atcc 51142 with as ligand. Full crystallographic information is available from OCA.

Reference

Characterization of two potentially universal turn motifs that shape the repeated five-residues fold--crystal structure of a lumenal pentapeptide repeat protein from Cyanothece 51142., Buchko GW, Ni S, Robinson H, Welsh EA, Pakrasi HB, Kennedy MA, Protein Sci. 2006 Nov;15(11):2579-95. PMID:17075135

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