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Gene regulating protein PDB id
2cro
Jmol
Contents
Protein chain
65 a.a. *
Waters ×17
* Residue conservation analysis
PDB id:
2cro
Name: Gene regulating protein
Title: Structure of phage 434 cro protein at 2.35 angstroms resolution
Structure: Regulatory protein cro. Chain: a. Engineered: yes
Source: Phage 434. Organism_taxid: 10712
Biol. unit: Trimer (from PQS)
Resolution:
2.35Å     R-factor:   0.195    
Authors: A.Mondragon,C.Wolberger,S.C.Harrison
Key ref: A.Mondragón et al. (1989). Structure of phage 434 Cro protein at 2.35 A resolution. J Mol Biol, 205, 179-188. PubMed id: 2647998 DOI: 10.1016/0022-2836(89)90374-4
Date:
08-Dec-88     Release date:   15-Oct-89    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P03036  (RCRO_BP434) -  Regulatory protein cro
Seq:
Struc: 		71 a.a.
65 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     regulation of transcription   3 terms 
  Biochemical function     DNA binding     3 terms  

 

 
DOI no: 10.1016/0022-2836(89)90374-4 J Mol Biol 205:179-188 (1989)
PubMed id: 2647998  
 
 
Structure of phage 434 Cro protein at 2.35 A resolution.
A.Mondragón, C.Wolberger, S.C.Harrison.
 
  ABSTRACT  
 
The crystal structure of phage 434 Cro protein has been determined and refined against 2.35 A data to an R-factor of 19.5%. The protein comprises five alpha-helices and shows the helix-turn-helix motif found in other repressor proteins.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
17296314 E.Shacham, B.Sheehan, and N.Volkmann (2007).
Density-based score for selecting near-native atomic models of unknown structures.
  J Struct Biol, 158, 188-195.  
15359276 S.Rumpel, A.Razeto, C.M.Pillar, V.Vijayan, A.Taylor, K.Giller, M.S.Gilmore, S.Becker, and M.Zweckstetter (2004).
Structure and DNA-binding properties of the cytolysin regulator CylR2 from Enterococcus faecalis.
  EMBO J, 23, 3632-3642.
PDB code: 1utx
15062080 T.Newlove, J.H.Konieczka, and M.H.Cordes (2004).
Secondary structure switching in Cro protein evolution.
  Structure, 12, 569-581.
PDB code: 1rzs
12511493 K.Fromknecht, P.D.Vogel, and J.G.Wise (2003).
Combinatorial redesign of the DNA binding specificity of a prokaryotic helix-turn-helix repressor.
  J Bacteriol, 185, 475-481.  
12598646 K.R.LeFevre, and M.H.Cordes (2003).
Retroevolution of lambda Cro toward a stable monomer.
  Proc Natl Acad Sci U S A, 100, 2345-2350.  
11913380 B.N.Dominy, and C.L.Brooks (2002).
Identifying native-like protein structures using physics-based potentials.
  J Comput Chem, 23, 147-160.  
11076539 D.V.Laurents, S.Corrales, M.Elías-Arnanz, P.Sevilla, M.Rico, and S.Padmanabhan (2000).
Folding kinetics of phage 434 Cro protein.
  Biochemistry, 39, 13963-13973.  
10842336 J.Higo, H.Kono, H.Nakamura, and A.Sarai (2000).
Solvent density and long-range dipole field around a DNA-binding protein studied by molecular dynamics.
  Proteins, 40, 193-206.  
9990839 J.A.Trulson, and G.L.Millhauser (1999).
The effect of mutations on peptide models of the DNA binding helix of p53: evidence for a correlation between structure and tumorigenesis.
  Biopolymers, 49, 215-224.  
  10452612 S.Padmanabhan, M.A.Jiménez, and M.Rico (1999).
Folding propensities of synthetic peptide fragments covering the entire sequence of phage 434 Cro protein.
  Protein Sci, 8, 1675-1688.  
  9514257 R.Aurora, and G.D.Rose (1998).
Helix capping.
  Protein Sci, 7, 21-38.  
9032054 M.A.Kercher, P.Lu, and M.Lewis (1997).
Lac repressor-operator complex.
  Curr Opin Struct Biol, 7, 76-85.  
  9000009 D.A.Erlanson, M.Chytil, and G.L.Verdine (1996).
The leucine zipper domain controls the orientation of AP-1 in the NFAT.AP-1.DNA complex.
  Chem Biol, 3, 981-991.  
8880931 H.Wako, M.Tachikawa, and A.Ogawa (1996).
A comparative study of dynamic structures between phage 434 Cro and repressor proteins by normal mode analysis.
  Proteins, 26, 72-80.  
  8599943 M.Suckow, M.Lopata, A.Seydel, B.Kisters-Woike, B.von Wilcken-Bergmann, and B.Müller-Hill (1996).
Mutant bZip-DNA complexes with four quasi-identical protein-DNA interfaces.
  EMBO J, 15, 598-606.  
  8535237 J.R.Desjarlais, and T.M.Handel (1995).
De novo design of the hydrophobic cores of proteins.
  Protein Sci, 4, 2006-2018.  
  7579657 J.R.Desjarlais, and T.M.Handel (1995).
New strategies in protein design.
  Curr Opin Biotechnol, 6, 460-466.  
  8563626 S.Y.Chung, and S.Subbiah (1995).
The use of side-chain packing methods in modeling bacteriophage repressor and cro proteins.
  Protein Sci, 4, 2300-2309.  
  8590003 T.E.Strzelecka, G.M.Clore, and A.M.Gronenborn (1995).
The solution structure of the Mu Ner protein reveals a helix-turn-helix DNA recognition motif.
  Structure, 3, 1087-1095.
PDB codes: 1neq 1ner
  8076591 R.H.Fogh, G.Ottleben, H.Rüterjans, M.Schnarr, R.Boelens, and R.Kaptein (1994).
Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy.
  EMBO J, 13, 3936-3944.
PDB codes: 1lea 1leb
  7849602 S.E.Brenner, and A.Berry (1994).
A quantitative methodology for the de novo design of proteins.
  Protein Sci, 3, 1871-1882.  
  7987224 T.Liu, E.F.DeRose, and G.P.Mullen (1994).
Determination of the structure of the DNA binding domain of gamma delta resolvase in solution.
  Protein Sci, 3, 1286-1295.
PDB codes: 1res 1ret
  8081737 D.W.Rodgers, and S.C.Harrison (1993).
The complex between phage 434 repressor DNA-binding domain and operator site OR3: structural differences between consensus and non-consensus half-sites.
  Structure, 1, 227-240.
PDB code: 1per
8290361 M.P.Laget, I.Callebaut, Y.de Launoit, D.Stehelin, and J.P.Mornon (1993).
Predicted common structural features of DNA-binding domains from Ets, Myb and HMG transcription factors.
  Nucleic Acids Res, 21, 5987-5996.  
8516313 S.A.Bustos, and R.F.Schleif (1993).
Functional domains of the AraC protein.
  Proc Natl Acad Sci U S A, 90, 5638-5642.  
1631139 K.Ogata, H.Hojo, S.Aimoto, T.Nakai, H.Nakamura, A.Sarai, S.Ishii, and Y.Nishimura (1992).
Solution structure of a DNA-binding unit of Myb: a helix-turn-helix-related motif with conserved tryptophans forming a hydrophobic core.
  Proc Natl Acad Sci U S A, 89, 6428-6432.  
1409566 R.Baumeister, G.Müller, B.Hecht, and W.Hillen (1992).
Functional roles of amino acid residues involved in forming the alpha-helix-turn-alpha-helix operator DNA binding motif of Tet repressor from Tn10.
  Proteins, 14, 168-177.  
2408042 H.C.Pace, P.Lu, and M.Lewis (1990).
lac repressor: crystallization of intact tetramer and its complexes with inducer and operator DNA.
  Proc Natl Acad Sci U S A, 87, 1870-1873.  
2672451 R.G.Brennan, and B.W.Matthews (1989).
Structural basis of DNA-protein recognition.
  Trends Biochem Sci, 14, 286-290.  
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 code is shown on the right.