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Transferase PDB id
1g3g
Jmol
Contents
Protein chain
164 a.a. *
* Residue conservation analysis
PDB id:
1g3g
Name: Transferase
Title: Nmr structure of the fha1 domain of yeast rad53
Structure: Protien kinase spk1. Chain: a. Fragment: the n-terminal fha domain (fha1), residues 1-164. Synonym: serine-protein kinase 1. Engineered: yes. Mutation: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: spk1 or rad53. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
NMR struc: 20 models
Authors: C.Yuan,H.Liao,M.Su,S.Yongkiettrakul,I.-J.L.Byeon,M.-D.Tsai
Key ref: H.Liao et al. (2000). Structure of the FHA1 domain of yeast Rad53 and identification of binding sites for both FHA1 and its target protein Rad9. J Mol Biol, 304, 941-951. PubMed id: 11124038 DOI: 10.1006/jmbi.2000.4291
Date:
24-Oct-00     Release date:   10-Jan-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P22216  (RAD53_YEAST) -  Serine/threonine-protein kinase RAD53
Seq:
Struc: 		 
Seq:
Struc: 		821 a.a.
164 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.7.11.1  - Non-specific serine/threonine protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
ATP
 + protein
 = ADP
 + phosphoprotein
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1006/jmbi.2000.4291 J Mol Biol 304:941-951 (2000)
PubMed id: 11124038  
 
 
Structure of the FHA1 domain of yeast Rad53 and identification of binding sites for both FHA1 and its target protein Rad9.
H.Liao, C.Yuan, M.I.Su, S.Yongkiettrakul, D.Qin, H.Li, I.J.Byeon, D.Pei, M.D.Tsai.
 
  ABSTRACT  
 
Forkhead-associated (FHA) domains have been shown to recognize both pThr and pTyr-peptides. The solution structures of the FHA2 domain of Rad53 from Saccharomyces cerevisiae, and its complex with a pTyr peptide, have been reported recently. We now report the solution structure of the other FHA domain of Rad53, FHA1 (residues 14-164), and identification of binding sites of FHA1 and its target protein Rad9. The FHA1 structure consists of 11 beta-strands, which form two large twisted anti-parallel beta-sheets folding into a beta-sandwich. Three short alpha-helices were also identified. The beta-strands are linked by several loops and turns. These structural features of free FHA1 are similar to those of free FHA2, but there are significant differences in the against FHA1 revealed an absolute requirement for Asp at the +3 position and a preference for Ala at the +2 position. These two criteria are met by a pThr motif (192)TEAD(195) in Rad9. Surface plasmon resonance analysis showed that a pThr peptide containing this motif, (188)SLEV(pT)EADATFVQ(200) from Rad9, binds to FHA1 with a K(d) value of 0.36 microM. Other peptides containing pTXXD sequences also bound to FHA1, but less tightly (K(d)=4-70 microM). These results suggest that Thr192 of Rad9 is the likely phosphorylation site recognized by the FHA1 domain of Rad53. The tight-binding peptide was then used to identify residues of FHA1 involved in the interaction with the pThr peptide. The results are compared with the interactions between the FHA2 domain and a pTyr peptide derived from Rad9 reported previously.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19081057 C.C.Lin, Y.S.Huoh, K.R.Schmitz, L.E.Jensen, and K.M.Ferguson (2008).
Pellino proteins contain a cryptic FHA domain that mediates interaction with phosphorylated IRAK1.
  Structure, 16, 1806-1816.
PDB codes: 3ega 3egb
18253837 H.Kumeta, K.Ogura, S.Adachi, Y.Fujioka, N.Tanuma, K.Tanuma, K.Kikuchi, and F.Inagaki (2008).
The NMR structure of the NIPP1 FHA domain.
  J Biomol NMR, 40, 219-224.
PDB code: 2jpe
  18473721 N.K.Bernstein, F.Karimi-Busheri, A.Rasouli-Nia, R.Mani, G.Dianov, J.N.Glover, and M.Weinfeld (2008).
Polynucleotide kinase as a potential target for enhancing cytotoxicity by ionizing radiation and topoisomerase I inhibitors.
  Anticancer Agents Med Chem, 8, 358-367.  
18656966 X.Liang, and S.R.Van Doren (2008).
Mechanistic insights into phosphoprotein-binding FHA domains.
  Acc Chem Res, 41, 991-999.  
17325030 G.Guillemain, E.Ma, S.Mauger, S.Miron, R.Thai, R.Guérois, F.Ochsenbein, and M.C.Marsolier-Kergoat (2007).
Mechanisms of checkpoint kinase Rad53 inactivation after a double-strand break in Saccharomyces cerevisiae.
  Mol Cell Biol, 27, 3378-3389.  
15770685 A.Traven, and J.Heierhorst (2005).
SQ/TQ cluster domains: concentrated ATM/ATR kinase phosphorylation site regions in DNA-damage-response proteins.
  Bioessays, 27, 397-407.  
16244663 I.J.Byeon, H.Li, H.Song, A.M.Gronenborn, and M.D.Tsai (2005).
Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67.
  Nat Struct Mol Biol, 12, 987-993.
PDB code: 2aff
15710546 J.Iwashita, Y.Sato, S.Kobayashi, T.Takeuchi, and T.Abe (2005).
Isolation and functional analysis of a chk2 homologue from Entamoeba histolytica.
  Parasitol Int, 54, 21-27.  
16285867 J.M.Daley, P.L.Palmbos, D.Wu, and T.E.Wilson (2005).
Nonhomologous end joining in yeast.
  Annu Rev Genet, 39, 431-451.  
16042389 Z.Ding, G.I.Lee, X.Liang, F.Gallazzi, A.Arunima, and S.R.Van Doren (2005).
PhosphoThr peptide binding globally rigidifies much of the FHA domain from Arabidopsis receptor kinase-associated protein phosphatase.
  Biochemistry, 44, 10119-10134.  
15271990 B.L.Pike, N.Tenis, and J.Heierhorst (2004).
Rad53 kinase activation-independent replication checkpoint function of the N-terminal forkhead-associated (FHA1) domain.
  J Biol Chem, 279, 39636-39644.  
15173168 K.Tanaka, and P.Russell (2004).
Cds1 phosphorylation by Rad3-Rad26 kinase is mediated by forkhead-associated domain interaction with Mrc1.
  J Biol Chem, 279, 32079-32086.  
15135525 V.Molle, D.Soulat, J.M.Jault, C.Grangeasse, A.J.Cozzone, and J.F.Prost (2004).
Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis.
  FEMS Microbiol Lett, 234, 215-223.  
12805372 B.L.Pike, S.Yongkiettrakul, M.D.Tsai, and J.Heierhorst (2003).
Diverse but overlapping functions of the two forkhead-associated (FHA) domains in Rad53 checkpoint kinase activation.
  J Biol Chem, 278, 30421-30424.  
12667463 C.Leroy, S.E.Lee, M.B.Vaze, F.Ochsenbien, R.Guerois, J.E.Haber, and M.C.Marsolier-Kergoat (2003).
PP2C phosphatases Ptc2 and Ptc3 are required for DNA checkpoint inactivation after a double-strand break.
  Mol Cell, 11, 827-835.  
14500786 G.I.Lee, Z.Ding, J.C.Walker, and S.R.Van Doren (2003).
NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase.
  Proc Natl Acad Sci U S A, 100, 11261-11266.
PDB codes: 1mzk 1n4t
12730380 Y.Zhu, J.Dai, P.G.Fuerst, and D.F.Voytas (2003).
Controlling integration specificity of a yeast retrotransposon.
  Proc Natl Acad Sci U S A, 100, 5891-5895.  
11953437 A.Hammet, B.L.Pike, and J.Heierhorst (2002).
Posttranscriptional regulation of the RAD5 DNA repair gene by the Dun1 kinase and the Pan2-Pan3 poly(A)-nuclease complex contributes to survival of replication blocks.
  J Biol Chem, 277, 22469-22474.  
12441400 B.P.Duncker, K.Shimada, M.Tsai-Pflugfelder, P.Pasero, and S.M.Gasser (2002).
An N-terminal domain of Dbf4p mediates interaction with both origin recognition complex (ORC) and Rad53p and can deregulate late origin firing.
  Proc Natl Acad Sci U S A, 99, 16087-16092.  
  12121644 E.S.Stavridi, Y.Huyen, I.R.Loreto, D.M.Scolnick, T.D.Halazonetis, N.P.Pavletich, and P.D.Jeffrey (2002).
Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein and its complex with tungstate.
  Structure, 10, 891-899.
PDB codes: 1lgp 1lgq
12386164 J.Ahn, and C.Prives (2002).
Checkpoint kinase 2 (Chk2) monomers or dimers phosphorylate Cdc25C after DNA damage regardless of threonine 68 phosphorylation.
  J Biol Chem, 277, 48418-48426.  
12024051 X.Xu, L.M.Tsvetkov, and D.F.Stern (2002).
Chk2 activation and phosphorylation-dependent oligomerization.
  Mol Cell Biol, 22, 4419-4432.  
11746948 R.L.Rich, and D.G.Myszka (2001).
Survey of the year 2000 commercial optical biosensor literature.
  J Mol Recognit, 14, 273-294.  
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.