2ZA4: Crystal Structural Analysis Of Barnase-barstar Complex

Citation:
Abstract
The complex of barnase (bn) and barstar (bs), which has been widely studied as a model for quantitative analysis of protein-protein interactions, is significantly destabilized by a single mutation, namely, bs Asp39 --> Ala, which corresponds to a change of 7.7 kcal x mol(-1) in the free energy of binding. However, there has been no structural information available to explain such a drastic destabilization. In the present study, we determined the structure of the mutant complex at 1.58 A resolution by X-ray crystallography. The complex was similar to the wild-type complex in terms of overall and interface structures; however, the hydrogen bond network mediated by water molecules at the interface was significantly different. Several water molecules filled the cavity created by the mutation and consequently caused rearrangement of the hydrated water molecules at the interface. The water molecules were redistributed into a channel-like structure that penetrated into the complex. Furthermore, molecular dynamics simulations showed that the mutation increased the mobility of water molecules at the interface. Since such a drastic change in hydration was not observed in other mutant complexes of bn and bs, the significant destabilization of the interaction may be due to this channel-like structure of hydrated water molecules.
PDB ID: 2ZA4Download
MMDB ID: 64533
PDB Deposition Date: 2007/10/1
Updated in MMDB: 2008/06
Experimental Method:
x-ray diffraction
Resolution: 1.58  Å
Source Organism:
Similar Structures:
Biological Unit for 2ZA4: dimeric; determined by author
Molecular Components in 2ZA4
Label Count Molecule
Proteins (2 molecules)
1
Ribonuclease
Molecule annotation
1
Barstar
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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