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PDBsum entry 1mq1
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protein Protein-protein interface(s) links
Metal binding protein PDB id
1mq1

 

 

 

 

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Contents
Protein chains
91 a.a. *
12 a.a. *
* Residue conservation analysis
PDB id:
1mq1
Name: Metal binding protein
Title: Ca2+-s100b-trtk-12 complex
Structure: S-100 protein, beta chain. Chain: a, b. Engineered: yes. F-actin capping protein alpha-1 subunit. Chain: c, d. Fragment: trtk-12 peptide, residues 265-276. Synonym: capz alpha-1, trtk-12 peptide. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: s100beta. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: the peptide is chemically synthesized.
NMR struc: 17 models
Authors: K.A.Mcclintock,G.S.Shaw
Key ref:
K.A.McClintock and G.S.Shaw (2003). A novel S100 target conformation is revealed by the solution structure of the Ca2+-S100B-TRTK-12 complex. J Biol Chem, 278, 6251-6257. PubMed id: 12480931 DOI: 10.1074/jbc.M210622200
Date:
13-Sep-02     Release date:   25-Dec-02    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P04271  (S100B_HUMAN) -  Protein S100-B from Homo sapiens
Seq:
Struc: 		92 a.a.
91 a.a.
Protein chains
Pfam   ArchSchema ?
P52907  (CAZA1_HUMAN) -  F-actin-capping protein subunit alpha-1 from Homo sapiens
Seq:
Struc: 		286 a.a.
12 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1074/jbc.M210622200 J Biol Chem 278:6251-6257 (2003)
PubMed id: 12480931  
 
 
A novel S100 target conformation is revealed by the solution structure of the Ca2+-S100B-TRTK-12 complex.
K.A.McClintock, G.S.Shaw.
 
  ABSTRACT  
 
The Alzheimer-linked neural protein S100B is a signaling molecule shown to control the assembly of intermediate filament proteins in a calcium-sensitive manner. Upon binding calcium, a conformational change occurs in S100B exposing a hydrophobic surface for target protein interactions. The synthetic peptide TRTK-12 (TRTKIDWNKILS), derived from random bacteriophage library screening, bears sequence similarity to several intermediate filament proteins and has the highest calcium-dependent affinity of any target molecule for S100B to date (K(d) <1 microm). In this work, the three-dimensional structure of the Ca(2+)-S100B-TRTK-12 complex has been determined by NMR spectroscopy. The structure reveals an extended, contiguous hydrophobic surface is formed on Ca(2+)-S100B for target interaction. The TRTK-12 peptide adopts a coiled structure that fits into a portion of this surface, anchored at Trp(7), and interacts with multiple hydrophobic contacts in helices III and IV of Ca(2+)-S100B. This interaction is strikingly different from the alpha-helical structures found for other S100 target peptides. By using the TRTK-12 interaction as a guide, in combination with other available S100 target structures, a recognition site on helix I is identified that may act in concert with the TRTK-12-binding site from helices III and IV. This would provide a larger, more complex site to interact with full-length target proteins and would account for the promiscuity observed for S100B target protein interactions.
 
  Selected figure(s)  
 
Figure 2.
Fig. 2. Structure of the Ca^2+-S100B-TRTK-12 complex. The N and C termini are labeled for one S100 monomer and TRTK-12, and helices are indicated for S100 . A, stereo view of the backbone superposition of the final ensemble of 17 NMR derived structures of the complex. S100 monomers are shown in magenta and blue, and the TRTK-12 peptide molecules are shown in light blue. B, ribbon structure of the complex. Each monomer consists of four -helices (helix I, blue; II, magenta; III, green; and IV, yellow) and two anti-parallel -strands (orange, blue). TRTK-12 is shown in dark blue. 		Figure 5.
Fig. 5. Electrostatic potential surface showing the TRTK-12-binding site on Ca^2+-S100B. Negative potential is indicated in blue, and positive potential is shown in red for Ca^2+-S100B. A, location of the two TRTK-12 molecules ( green) on opposite sides of Ca^2+-S100B. The TRTK-12 peptide fits into the hydrophobic cleft generated by helices III and IV of each monomer. Note that on either side of the TRTK-12-binding site a significant uncharged region exists. B, environment of the anchoring Trp7 residue from TRTK-12 (green) showing interactions with S100B residues (blue) in helix III (Val56 and Thr59) and IV (Phe^76 and Val80).
 
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2003, 278, 6251-6257) copyright 2003.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20950652 T.Ostendorp, J.Diez, C.W.Heizmann, and G.Fritz (2011).
The crystal structures of human S100B in the zinc- and calcium-loaded state at three pH values reveal zinc ligand swapping.
  Biochim Biophys Acta, 1813, 1083-1091.
PDB codes: 3czt 3d0y 3d10
  20827422 D.B.Zimmer, and D.J.Weber (2010).
The Calcium-Dependent Interaction of S100B with Its Protein Targets.
  Cardiovasc Psychiatry Neurol, 2010, 0.  
20053360 T.H.Charpentier, L.E.Thompson, M.A.Liriano, K.M.Varney, P.T.Wilder, E.Pozharski, E.A.Toth, and D.J.Weber (2010).
The effects of CapZ peptide (TRTK-12) binding to S100B-Ca2+ as examined by NMR and X-ray crystallography.
  J Mol Biol, 396, 1227-1243.
PDB codes: 3iqo 3iqq
19827097 A.Rezvanpour, J.M.Phillips, and G.S.Shaw (2009).
Design of high-affinity S100-target hybrid proteins.
  Protein Sci, 18, 2528-2536.  
18650434 N.T.Wright, B.L.Prosser, K.M.Varney, D.B.Zimmer, M.F.Schneider, and D.J.Weber (2008).
S100A1 and calmodulin compete for the same binding site on ryanodine receptor.
  J Biol Chem, 283, 26676-26683.
PDB code: 2k2f
18558076 X.Shang, H.Cheng, and R.Zhou (2008).
Chromosomal mapping, differential origin and evolution of the S100 gene family.
  Genet Sel Evol, 40, 449-464.  
18803400 Y.T.Lee, Y.N.Dimitrova, G.Schneider, W.B.Ridenour, S.Bhattacharya, S.E.Soss, R.M.Caprioli, A.Filipek, and W.J.Chazin (2008).
Structure of the S100A6 complex with a fragment from the C-terminal domain of Siah-1 interacting protein: a novel mode for S100 protein target recognition.
  Biochemistry, 47, 10921-10932.
PDB code: 2jtt
17713798 A.Gieldon, M.Mori, and R.Del Conte (2007).
Theoretical study on binding of S100B protein.
  J Mol Model, 13, 1123-1131.  
17159909 K.C.Lee, and R.L.Eckert (2007).
S100A7 (Psoriasin)--mechanism of antibacterial action in wounds.
  J Invest Dermatol, 127, 945-957.  
17660747 T.Ostendorp, E.Leclerc, A.Galichet, M.Koch, N.Demling, B.Weigle, C.W.Heizmann, P.M.Kroneck, and G.Fritz (2007).
Structural and functional insights into RAGE activation by multimeric S100B.
  EMBO J, 26, 3868-3878.
PDB code: 2h61
16766622 V.Sivaraja, T.K.Kumar, D.Rajalingam, I.Graziani, I.Prudovsky, and C.Yu (2006).
Copper binding affinity of S100A13, a key component of the FGF-1 nonclassical copper-dependent release complex.
  Biophys J, 91, 1832-1843.  
15191538 R.L.Eckert, A.M.Broome, M.Ruse, N.Robinson, D.Ryan, and K.Lee (2004).
S100 proteins in the epidermis.
  J Invest Dermatol, 123, 23-33.  
12842051 A.C.Dempsey, M.P.Walsh, and G.S.Shaw (2003).
Unmasking the annexin I interaction from the structure of Apo-S100A11.
  Structure, 11, 887-897.
PDB code: 1nsh
14661952 S.Bhattacharya, E.Large, C.W.Heizmann, B.Hemmings, and W.J.Chazin (2003).
Structure of the Ca2+/S100B/NDR kinase peptide complex: insights into S100 target specificity and activation of the kinase.
  Biochemistry, 42, 14416-14426.
PDB code: 1psb
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.

 

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