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PDBsum entry 1z1c

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protein dna_rna ligands metals links
Virus/DNA PDB id
1z1c

 

 

 

 

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Contents
Protein chain
549 a.a. *
DNA/RNA
Ligands
D5M
Metals
_CA ×2
Waters ×101
* Residue conservation analysis
PDB id:
1z1c
Name: Virus/DNA
Title: Structural determinants of tissue tropism and in vivo pathogenicity for the parvovirus minute virus of mice
Structure: 5'-d( Ap Tp Cp Cp Tp Cp Tp Ap Tp Cp Ap C)-3'. Chain: b. Engineered: yes. 5'-d( Ap Cp Ap Cp Cp Ap Ap Ap A)-3'. Chain: c. Engineered: yes. Coat protein vp2. Chain: a. Engineered: yes
Source: Synthetic: yes. Murine minute virus (strain mvmi). Organism_taxid: 10795. Strain: mvmi. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9.
Resolution:
3.50Å     R-factor:   0.325     R-free:   0.329
Authors: M.Kontou,L.Govindasamy,H.J.Nam,N.Bryant,A.L.Llamas-Saiz,C.Foces- Foces,E.Hernando,M.P.Rubio,R.Mckenna,J.M.Almendral,M.Agbandje- Mckenna
Key ref: M.Kontou et al. (2005). Structural determinants of tissue tropism and in vivo pathogenicity for the parvovirus minute virus of mice. J Virol, 79, 10931-10943. PubMed id: 16103145
Date:
03-Mar-05     Release date:   06-Sep-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P07302  (CAPSD_MUMIM) -  Capsid protein VP1 from Murine minute virus (strain MVMi)
Seq:
Struc:
 
Seq:
Struc:
729 a.a.
549 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DNA/RNA chains
  A-T-C-C-T-C-T-A-T-C-A-C 12 bases
  A-C-A-C-C-A-A-A-A 9 bases

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
J Virol 79:10931-10943 (2005)
PubMed id: 16103145  
 
 
Structural determinants of tissue tropism and in vivo pathogenicity for the parvovirus minute virus of mice.
M.Kontou, L.Govindasamy, H.J.Nam, N.Bryant, A.L.Llamas-Saiz, C.Foces-Foces, E.Hernando, M.P.Rubio, R.McKenna, J.M.Almendral, M.Agbandje-McKenna.
 
  ABSTRACT  
 
Two strains of the parvovirus minute virus of mice (MVM), the immunosuppressive (MVMi) and the prototype (MVMp) strains, display disparate in vitro tropism and in vivo pathogenicity. We report the crystal structures of MVMp virus-like particles (MVMp(b)) and native wild-type (wt) empty capsids (MVMp(e)), determined and refined to 3.25 and 3.75 A resolution, respectively, and their comparison to the structure of MVMi, also refined to 3.5 A resolution in this study. A comparison of the MVMp(b) and MVMp(e) capsids showed their structures to be the same, providing structural verification that some heterologously expressed parvovirus capsids are indistinguishable from wt capsids produced in host cells. The structures of MVMi and MVMp capsids were almost identical, but local surface conformational differences clustered from symmetry-related capsid proteins at three specific domains: (i) the icosahedral fivefold axis, (ii) the "shoulder" of the protrusion at the icosahedral threefold axis, and (iii) the area surrounding the depression at the icosahedral twofold axis. The latter two domains contain important determinants of MVM in vitro tropism (residues 317 and 321) and forward mutation residues (residues 399, 460, 553, and 558) conferring fibrotropism on MVMi. Furthermore, these structural differences between the MVM strains colocalize with tropism and pathogenicity determinants mapped for other autonomous parvovirus capsids, highlighting the importance of common parvovirus capsid regions in the control of virus-host interactions.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20923881 M.G.Mateu (2011).
Virus engineering: functionalization and stabilization.
  Protein Eng Des Sel, 24, 53-63.  
20375175 B.L.Gurda, K.N.Parent, H.Bladek, R.S.Sinkovits, M.A.Dimattia, C.Rence, A.Castro, R.McKenna, N.Olson, K.Brown, T.S.Baker, and M.Agbandje-McKenna (2010).
Human bocavirus capsid structure: insights into the structural repertoire of the parvoviridae.
  J Virol, 84, 5880-5889.  
20223221 K.N.Parent, R.Khayat, L.H.Tu, M.M.Suhanovsky, J.R.Cortines, C.M.Teschke, J.E.Johnson, and T.S.Baker (2010).
P22 coat protein structures reveal a novel mechanism for capsid maturation: stability without auxiliary proteins or chemical crosslinks.
  Structure, 18, 390-401.
PDB codes: 3iyh 3iyi
19939915 L.Riolobos, N.Valle, E.Hernando, B.Maroto, M.Kann, and J.M.Almendral (2010).
Viral oncolysis that targets Raf-1 signaling control of nuclear transport.
  J Virol, 84, 2090-2099.  
19955311 S.F.Cotmore, S.Hafenstein, and P.Tattersall (2010).
Depletion of virion-associated divalent cations induces parvovirus minute virus of mice to eject its genome in a 3'-to-5' direction from an otherwise intact viral particle.
  J Virol, 84, 1945-1956.  
19307554 C.Carrasco, M.Douas, R.Miranda, M.Castellanos, P.A.Serena, J.L.Carrascosa, M.G.Mateu, M.I.Marqués, and P.J.de Pablo (2009).
The capillarity of nanometric water menisci confined inside closed-geometry viral cages.
  Proc Natl Acad Sci U S A, 106, 5475-5480.  
18045943 A.López-Bueno, J.C.Segovia, J.A.Bueren, M.G.O'Sullivan, F.Wang, P.Tattersall, and J.M.Almendral (2008).
Evolution to pathogenicity of the parvovirus minute virus of mice in immunodeficient mice involves genetic heterogeneity at the capsid domain that determines tropism.
  J Virol, 82, 1195-1203.  
18508892 B.Kaufmann, P.R.Chipman, V.A.Kostyuchenko, S.Modrow, and M.G.Rossmann (2008).
Visualization of the externalized VP2 N termini of infectious human parvovirus B19.
  J Virol, 82, 7306-7312.  
18334651 C.Carrasco, M.Castellanos, P.J.de Pablo, and M.G.Mateu (2008).
Manipulation of the mechanical properties of a virus by protein engineering.
  Proc Natl Acad Sci U S A, 105, 4150-4155.  
17626084 B.Kaufmann, A.López-Bueno, M.G.Mateu, P.R.Chipman, C.D.Nelson, C.R.Parrish, J.M.Almendral, and M.G.Rossmann (2007).
Minute virus of mice, a parvovirus, in complex with the Fab fragment of a neutralizing monoclonal antibody.
  J Virol, 81, 9851-9858.  
17728238 H.J.Nam, M.D.Lane, E.Padron, B.Gurda, R.McKenna, E.Kohlbrenner, G.Aslanidi, B.Byrne, N.Muzyczka, S.Zolotukhin, and M.Agbandje-McKenna (2007).
Structure of adeno-associated virus serotype 8, a gene therapy vector.
  J Virol, 81, 12260-12271.
PDB code: 2qa0
16415031 A.López-Bueno, M.P.Rubio, N.Bryant, R.McKenna, M.Agbandje-McKenna, and J.M.Almendral (2006).
Host-selected amino acid changes at the sialic acid binding pocket of the parvovirus capsid modulate cell binding affinity and determine virulence.
  J Virol, 80, 1563-1573.  
16945903 C.Carrasco, A.Carreira, I.A.Schaap, P.A.Serena, J.Gómez-Herrero, M.G.Mateu, and P.J.de Pablo (2006).
DNA-mediated anisotropic mechanical reinforcement of a virus.
  Proc Natl Acad Sci U S A, 103, 13706-13711.  
16971437 L.Govindasamy, E.Padron, R.McKenna, N.Muzyczka, N.Kaludov, J.A.Chiorini, and M.Agbandje-McKenna (2006).
Structurally mapping the diverse phenotype of adeno-associated virus serotype 4.
  J Virol, 80, 11556-11570.
PDB code: 2g8g
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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