PDBsum entry 2g0y

Unknown function

PDB id

2g0y

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Contents

			Protein chain

					133 a.a. *

			Metals

					_CA ×3

			Waters ×16

* Residue conservation analysis

PDB id:

2g0y

Links

Name:

Unknown function

Title:

Crystal structure of a lumenal pentapeptide repeat protein from cyanothece sp 51142 at 2.3 angstrom resolution. Tetragonal crystal form

Structure:

Pentapeptide repeat protein. Chain: a. Fragment: full-length pentapeptide repeat protein minus n-terminal 29 residues predicted to be a signal peptide. Engineered: yes

Source:

Cyanothece sp. Atcc 51142. Organism_taxid: 43989. Atcc: 51142. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Tetramer (from PQS)

Resolution:

2.30Å

R-factor:

0.233

R-free:

0.266

Authors:

M.A.Kennedy,S.Ni,G.W.Buchko,H.Robinson

Key ref:

G.W.Buchko et al. (2006). 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. Protein Sci, 15, 2579-2595. PubMed id: 17075135 DOI: 10.1110/ps.062407506

Date:

13-Feb-06

Release date:

07-Nov-06

PROCHECK

	Headers

	References

Protein chain

B1WVN5 (RFR32_CYAA5) - Pentapeptide repeat protein Rfr32 from Crocosphaera subtropica (strain ATCC 51142 / BH68)

Seq: Struc:					179 a.a. 133 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1110/ps.062407506	Protein Sci 15:2579-2595 (2006)
PubMed id: 17075135

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.
G.W.Buchko, S.Ni, H.Robinson, E.A.Welsh, H.B.Pakrasi, M.A.Kennedy.

ABSTRACT

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.

Selected figure(s)



	Figure 10. Figure 10. Predicted residue composition of the 35 PRPs in Cyanothece

Figure was selected by an automated process.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21227918

X.Xiong, E.H.Bromley, P.Oelschlaeger, D.N.Woolfson, and J.Spencer (2011).
Structural insights into quinolone antibiotic resistance mediated by pentapeptide repeat proteins: conserved surface loops direct the activity of a Qnr protein from a Gram-negative bacterium.

Nucleic Acids Res, 39, 3917-3927.

PDB codes:

3pss 3psz

20661999

N.Yokoi, H.Inaba, M.Terauchi, A.Z.Stieg, N.J.Sanghamitra, T.Koshiyama, K.Yutani, S.Kanamaru, F.Arisaka, T.Hikage, A.Suzuki, T.Yamane, J.K.Gimzewski, Y.Watanabe, S.Kitagawa, and T.Ueno (2010).
Construction of robust bio-nanotubes using the controlled self-assembly of component proteins of bacteriophage T4.

Small, 6, 1873-1879.

PDB code:

3a1m

20932305

Q.Guo, J.Weng, X.Xu, M.Wang, X.Wang, X.Ye, W.Wang, and M.Wang (2010).
A mutational analysis and molecular dynamics simulation of quinolone resistance proteins QnrA1 and QnrC from Proteus mirabilis.

BMC Struct Biol, 10, 33.

19060136

A.Mérens, S.Matrat, A.Aubry, C.Lascols, V.Jarlier, C.J.Soussy, J.D.Cavallo, and E.Cambau (2009).
The pentapeptide repeat proteins MfpAMt and QnrB4 exhibit opposite effects on DNA gyrase catalytic reactions and on the ternary gyrase-DNA-quinolone complex.

J Bacteriol, 191, 1587-1594.

19390151

M.W.Vetting, S.S.Hegde, and J.S.Blanchard (2009).
Crystallization of a pentapeptide-repeat protein by reductive cyclic pentylation of free amines with glutaraldehyde.

Acta Crystallogr D Biol Crystallogr, 65, 462-469.

PDB code:

2w7z

17922649

G.B.Zavilgelsky, and S.M.Rastorguev (2007).
DNA mimicry by proteins as effective mechanism for regulation of activity of DNA-dependent enzymes.

Biochemistry (Mosc), 72, 913.

17142909

G.W.Buchko, H.Robinson, S.Ni, H.B.Pakrasi, and M.A.Kennedy (2006).
Cloning, expression, crystallization and preliminary crystallographic analysis of a pentapeptide-repeat protein (Rfr23) from the bacterium Cyanothece 51142.

Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 1251-1254.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.