 |
PDBsum entry 1fr2
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Immune system
|
PDB id
|
|
|
|
1fr2
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Crystal structure of the e9 dnase domain with a mutant immunity protein im9(e41a)
|
 |
|
Authors
|
 |
U.C.Kuhlmann,
A.J.Pommer,
G.M.Moore,
R.James,
C kleanthous,
A.M.Hemmings.
|
 |
|
Ref.
|
 |
To be Published ...
|
 |
 |
|
Secondary reference #1
|
 |
|
Title
|
 |
Specificity in protein-Protein interactions: the structural basis for dual recognition in endonuclease colicin-Immunity protein complexes.
|
 |
|
Authors
|
 |
U.C.Kühlmann,
A.J.Pommer,
G.R.Moore,
R.James,
C.Kleanthous.
|
 |
|
Ref.
|
 |
J Mol Biol, 2000,
301,
1163-1178.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
|
 |
 |
 |
|
 |
|
 |
Figure 4.
Figure 4. Hydrogen bonding interactions at the E9 DNase-Im9
interface. (a) and (b) show similar orientations of the
interface and are stereo representations in which Im9 is
coloured yellow with light side-chains and the DNase red with
dark side-chains. Details are given in Table 2 and Table 3. (a)
Direct hydrogen bonds between Im9 and the E9 DNase surrounding
the core of the interface, made up of a stacking interaction
between Tyr54 Im9 with Phe86 E9 DNase. (b) Water-mediated
hydrogen bonds.
|
 |
Figure 10.
Figure 10. Comparison of hydrogen bonding interactions to
conserved water molecules in the E7 DNase-Im7 (from [Ko et al
1999]), dark shading, and E9 DNase-Im9 complexes (present work),
light shading. With the exception of Asn90 (which is glutamine
in the E7 DNase), conserved side-chains and backbone atoms are
involved in coordinating the interfacial water molecules.
Hydrogen bonds and side-chain numbering are for the E9 DNase-Im9
complex.
|
 |
|
 |
 |
|
The above figures are
reproduced from the cited reference
with permission from Elsevier
|
 |
|
|
|
|
 |