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PDBsum entry 1dug

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protein ligands Protein-protein interface(s) links
Transferase, blood clotting PDB id
1dug
Jmol
Contents
Protein chains
234 a.a. *
Ligands
GSH ×2
Waters ×662
* Residue conservation analysis
PDB id:
1dug
Name: Transferase, blood clotting
Title: Structure of the fibrinogen g chain integrin binding and factor xiiia crosslinking sites obtained through carrier protein driven crystallization
Structure: Chimera of glutathione s-transferase-synthetic linker-c-terminal fibrinogen gamma chain. Chain: a, b. Engineered: yes. Other_details: glutathione s-transferase (residues 1-217) bound to synthetic sdp linker (residues 218-220) bound to c-terminal fibrinogen gamma chain (residues 221-234)
Source: Schistosoma japonicum. Organism_taxid: 6182. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: eukaryota. Metazoa. Platyhelminthes. Trematoda. Digenea. Strigeidida. Schistosomatoidea. Schistosomatidae. Schistosoma
Biol. unit: Dimer (from PQS)
Resolution:
1.80Å     R-factor:   0.185     R-free:   0.226
Authors: S.Ware,J.P.Donahue,J.Hawiger,W.F.Anderson
Key ref: S.Ware et al. (1999). Structure of the fibrinogen gamma-chain integrin binding and factor XIIIa cross-linking sites obtained through carrier protein driven crystallization. Protein Sci, 8, 2663-2671. PubMed id: 10631982 DOI: 10.1110/ps.8.12.2663
Date:
17-Jan-00     Release date:   02-Feb-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P08515  (GST26_SCHJA) -  Glutathione S-transferase class-mu 26 kDa isozyme
Seq:
Struc:
218 a.a.
234 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.5.1.18  - Glutathione transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RX + glutathione = HX + R-S-glutathione
RX
+
glutathione
Bound ligand (Het Group name = GSH)
corresponds exactly
= HX
+ R-S-glutathione
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     transferase activity     2 terms  

 

 
    reference    
 
 
DOI no: 10.1110/ps.8.12.2663 Protein Sci 8:2663-2671 (1999)
PubMed id: 10631982  
 
 
Structure of the fibrinogen gamma-chain integrin binding and factor XIIIa cross-linking sites obtained through carrier protein driven crystallization.
S.Ware, J.P.Donahue, J.Hawiger, W.F.Anderson.
 
  ABSTRACT  
 
The human fibrinogen gamma-chain C-terminal segment functions as the platelet integrin binding site as well as the Factor XIIIa cross-linking substrate and thus plays an important role in blood clot formation and stabilization. The three-dimensional structure of this segment has been determined using carrier protein driven crystallization. The C-terminal segment, gamma-(398-411), was attached to a linker sequence at the C-terminus of glutathione S-transferase and the structure of this fusion protein determined at 1.8 A resolution. Functional studies of the chimeric protein demonstrate that the fibrinogen sequence in the presence of the carrier protein retains its specific functions as ligand for platelet integrin alpha(IIb)beta3 (gpIIb/IIIa) and as a cross-linking substrate for Factor XIIIa. The structure obtained for the fibrinogen gamma-chain segment is not affected by crystal packing and can provide the missing links to the recently reported model of cross-linked fibrin.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  20606742 A.Cortelazzo, R.Guerranti, L.Bini, N.Hope-Onyekwere, C.Muzzi, R.Leoncini, and R.Pagani (2010).
Effects of snake venom proteases on human fibrinogen chains.
  Blood Transfus, 8, s120-s125.  
18780816 L.Corsini, M.Hothorn, K.Scheffzek, M.Sattler, and G.Stier (2008).
Thioredoxin as a fusion tag for carrier-driven crystallization.
  Protein Sci, 17, 2070-2079.  
18710925 T.A.Springer, J.Zhu, and T.Xiao (2008).
Structural basis for distinctive recognition of fibrinogen gammaC peptide by the platelet integrin alphaIIbbeta3.
  J Cell Biol, 182, 791-800.
PDB codes: 2vc2 2vdk 2vdl 2vdm 2vdn 2vdo 2vdp 2vdq 2vdr
17962407 S.Nauli, S.Farr, Y.J.Lee, H.Y.Kim, S.Faham, and J.U.Bowie (2007).
Polymer-driven crystallization.
  Protein Sci, 16, 2542-2551.
PDB codes: 2qar 2qb0 2qb1
12485987 C.C.Deivanayagam, E.R.Wann, W.Chen, M.Carson, K.R.Rajashankar, M.Höök, and S.V.Narayana (2002).
A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A.
  EMBO J, 21, 6660-6672.
PDB code: 1n67
12496082 M.V.Petoukhov, N.A.Eady, K.A.Brown, and D.I.Svergun (2002).
Addition of missing loops and domains to protein models by x-ray solution scattering.
  Biophys J, 83, 3113-3125.  
12162736 Z.Yang, G.Spraggon, L.Pandi, S.J.Everse, M.Riley, and R.F.Doolittle (2002).
Crystal structure of fragment D from lamprey fibrinogen complexed with the peptide Gly-His-Arg-Pro-amide.
  Biochemistry, 41, 10218-10224.
PDB code: 1lwu
11468358 R.R.Hantgan, M.Rocco, C.Nagaswami, and J.W.Weisel (2001).
Binding of a fibrinogen mimetic stabilizes integrin alphaIIbbeta3's open conformation.
  Protein Sci, 10, 1614-1626.  
11264588 Y.H.Han, Y.H.Chung, T.Y.Kim, S.J.Hong, J.D.Choi, and Y.J.Chung (2001).
Crystallization of Clonorchis sinensis 26 kDa glutathione S-transferase and its fusion proteins with peptides of different lengths.
  Acta Crystallogr D Biol Crystallogr, 57, 579-581.  
10828988 M.Moaddel, D.H.Farrell, M.A.Daugherty, and M.G.Fried (2000).
Interactions of human fibrinogens with factor XIII: roles of calcium and the gamma' peptide.
  Biochemistry, 39, 6698-6705.  
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.