.:3D Macromolecule:.

x
x

Supported by: RasMol n RCSB PDB

PRION BINDING PROTEIN

This 3D animation is (PBP) that are display with cartoon and color rainbow.

This is the structure of the Het -S N- Terminal Domain. Mutant.
It is small protein under Prion-Binding Protein(PBP), with 2WVQ database code.

HET-S (97% identical to HET-s) has an N-terminal globular domain that exerts a prion-inhibitory effect in cis on its own prion-forming domain (PFD) and in trans on HET-s prion propagation.

CLICK ON THE PIC! Picture of PBP in Assumed Biological Molecule. The other animation of PBP: with 4 choices to display (display, color, surface, and toggle) .

We show that HET-S fails to form fibrils in vitro and that it inhibits HET-s PFD fibrillization in trans. In vivo analyses indicate that beta-structuring of the HET-S PFD is required for HET-S activity.

The crystal structures of the globular domains of HET-s and HET-S NMR- are highly similar, comprising a helical fold, while based characterizations revealed no differences in the conformations of the PFDs.

The PBP is in stands and display in different temperature of the groups.

We conclude that prion inhibition is not encoded by structure but rather in stability and oligomerization properties: The molcule which is in strands and coloured when HET-S.This forms a prion seed or is
incorporated into a HET-s fibril via its PFD, the beta-structuring in this domain induces a change in its globular domain, generating a molecular species that is incompetent for fibril growth.

There are seven author of this molecule: Greenwarld, J., Buhtz, C., Ritter, C., KwiatkowskiW. Choe, S., Saupe, S.J, Riek, R. It was deposited on 19th October and released on 28th July one year later.

To be more specific, this Prion Binding Protein has 51222.88 in structure weight and 225 in length. It has only one polymer, polypeptide(L). Furthermore, it have A and B chains, which are N-Terminal domain and residues 13-221 and yes it has been mutate.

It can be found in Podospora anserina and with expression system of 'Escherichia coli'. Prion Binding Protein composed of 5 chains, 418(200) groups, 3363(214) atoms, 15 bonds, 24 helicals and 4 strands.

SULFOLOUS SOLFATARIUS P2

CLICK ON THE PIC! Picture of SULFOLOUS SOLFATARIUS P2 in asymmetric unit.The other animation of SULFOLOUS SOLFATARIUS P2: with 4 choices to display (display, color, surface, and toggle) . Have FUN exploring the structure of SULFOLOUS SOLFATARIUS P2

The shape of this molecules is like crystal and it is fun to watch the molecule with 3D. 2X3D is the database code of the molecule. It has 14 chains, with 720(11) groups, 5497(11) atoms, and 5520 bands..

Here is the experimental details of the molecule. It used X-RAY DIFFRACTION with resolution of 2.70. In addition, the R-Value is 0.227(obs.) and the R-Free is 0.247.

The cell unit are divided into two: length(A) and angle(degree)..Length of a = 151.09, b =82.98, c =69.86, while the angle are 90.00, 109.70, and 90.00 respectively.

If the molecule above(Prion Binding Protein) has seven author, SULFOLOBUS
SULFATARICUS P2 has eight authors. They are Oke, M., Carter, L.G, Johnson, K.A, Liu, H., Mcmahon, S.A, Mcewan, A.R, White, M.F., Naismith, J.H.
This is the molecule with backbone display and coloured in different group.

This molecule is deposited on 24th January and was released 28th July on the same year. This molecule has only one polymer, which is polypeptide(L) and 96 in length. Furthermore, the structure weight is 844418.40 with A, B, C, D, E, F, G, and H chains.The expression system of the molecule is 'Eschericia coli'.