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PDBsum entry 3hrz
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protein ligands metals Protein-protein interface(s) links
Immune system PDB id
3hrz

 

 

 

 

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Contents
Protein chains
614 a.a. *
233 a.a. *
362 a.a. *
693 a.a. *
Ligands
NAG-NAG
NAG ×3
P6G ×2
PO4 ×5
Metals
_MG ×2
__K
Waters ×751
* Residue conservation analysis
PDB id:
3hrz
Name: Immune system
Title: Cobra venom factor (cvf) in complex with human factor b
Structure: Cobra venom factor. Chain: a. Fragment: residues 23-649. Synonym: cvf, complement c3 homolog, cobra venom factor alpha chain, cobra venom factor gamma chain, cobra venom factor beta chain. Cobra venom factor. Chain: b. Fragment: residues 733-984. Synonym: cvf, complement c3 homolog, cobra venom factor alpha chain,
Source: Naja kaouthia. Organism_taxid: 8649. Other_details: cobra venom. Homo sapiens. Human. Organism_taxid: 9606. Gene: cfb, bf, bfd. Expressed in: homo sapiens. Expression_system_taxid: 9606.
Resolution:
2.20Å     R-factor:   0.181     R-free:   0.226
Authors: B.J.C.Janssen,L.Gomes,R.I.Koning,D.I.Svergun,A.J.Koster, D.C.Fritzinger,C.-W.Vogel,P.Gros
Key ref: B.J.Janssen et al. (2009). Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex. Embo J, 28, 2469-2478. PubMed id: 19574954
Date:
10-Jun-09     Release date:   07-Jul-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q91132  (VCO3_NAJKA) -  Cobra venom factor from Naja kaouthia
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1642 a.a.
614 a.a.
Protein chain
Pfam   ArchSchema ?
Q91132  (VCO3_NAJKA) -  Cobra venom factor from Naja kaouthia
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1642 a.a.
233 a.a.
Protein chain
Pfam   ArchSchema ?
Q91132  (VCO3_NAJKA) -  Cobra venom factor from Naja kaouthia
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1642 a.a.
362 a.a.
Protein chain
Pfam   ArchSchema ?
P00751  (CFAB_HUMAN) -  Complement factor B from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		764 a.a.
693 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain D: E.C.3.4.21.47  - alternative-complement-pathway C3/C5 convertase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Cleaves C3 in the alpha-chain to yield C3a and C3b. Cleaves C5 in the alpha-chain to yield C5a and C5b. Both cleavages take place at the C-terminal of an arginine residue.

 

 
Embo J 28:2469-2478 (2009)
PubMed id: 19574954  
 
 
Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex.
B.J.Janssen, L.Gomes, R.I.Koning, D.I.Svergun, A.J.Koster, D.C.Fritzinger, C.W.Vogel, P.Gros.
 
  ABSTRACT  
 
Immune protection by the complement system critically depends on assembly of C3 convertases on the surface of pathogens and altered host cells. These short-lived protease complexes are formed through pro-convertases, which for the alternative pathway consist of the complement component C3b and the pro-enzyme factor B (FB). Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases. FB is loaded onto CVF through its pro-peptide Ba segment by specific contacts, which explain the specificity for the homologous C3b over the native C3 and inactive products iC3b and C3c. The protease segment Bb binds the carboxy terminus of CVF through the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain. A possible dynamic equilibrium between a 'loading' and 'activation' state of the pro-convertase may explain the observed difference between the crystal structure of CVFB and the EM structure of C3bB. These insights into formation of convertases provide a basis for further development of complement therapeutics.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21352830 K.Kucera, L.M.Harrison, M.Cappello, and Y.Modis (2011).
Ancylostoma ceylanicum excretory-secretory protein 2 adopts a netrin-like fold and defines a novel family of nematode proteins.
  J Mol Biol, 408, 9.
PDB code: 3nsw
21217642 N.S.Laursen, K.R.Andersen, I.Braren, E.Spillner, L.Sottrup-Jensen, and G.R.Andersen (2011).
Substrate recognition by complement convertases revealed in the C5-cobra venom factor complex.
  EMBO J, 30, 606-616.
PDB codes: 3prx 3pvm
20467445 D.Serruto, R.Rappuoli, M.Scarselli, P.Gros, and J.A.van Strijp (2010).
Molecular mechanisms of complement evasion: learning from staphylococci and meningococci.
  Nat Rev Microbiol, 8, 393-399.  
21205667 F.Forneris, D.Ricklin, J.Wu, A.Tzekou, R.S.Wallace, J.D.Lambris, and P.Gros (2010).
Structures of C3b in complex with factors B and D give insight into complement convertase formation.
  Science, 330, 1816-1820.
PDB codes: 2xw9 2xwa 2xwb 2xwj
20876141 H.Chen, D.Ricklin, M.Hammel, B.L.Garcia, W.J.McWhorter, G.Sfyroera, Y.Q.Wu, A.Tzekou, S.Li, B.V.Geisbrecht, V.L.Woods, and J.D.Lambris (2010).
Allosteric inhibition of complement function by a staphylococcal immune evasion protein.
  Proc Natl Acad Sci U S A, 107, 17621-17626.  
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.

 

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