PDBsum entry 1vqc

DNA binding protein

PDB id: 1vqc

Contents

Protein chain

86 a.a.

Waters ×42

References listed in PDB file

Key reference

Title

Potential use of additivity of mutational effects in simplifying protein engineering.

Authors

M.M.Skinner, T.C.Terwilliger.

Ref.

Proc Natl Acad Sci U S A, 1996, 93, 10753-10757.

PubMed id

8855252

Note: In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above were obtained from the PDBe's Unpublished References server.

Abstract

The problem of rationally engineering protein molecules can be simplified where effects of mutations on protein function are additive. Crystal structures of single and double mutants in the hydrophobic core of gene V protein indicate that structural and functional effects of core mutations are additive when the regions structurally influenced by the mutations do not substantially overlap. These regions of influence can provide a simple basis for identifying sets of mutations that will show additive effects.

Secondary reference #1

Title

Difference refinement: obtaining differences between two related structures.

Authors

T.C.Terwilliger, J.Berendzen.

Ref.

Acta Crystallogr D Biol Crystallogr, 1995, 51, 609-618. [DOI no: 10.1107/S0907444994013247]

PubMed id

15299790

Figure 1.
Fig. 1. The effects of incompleteness of data on model quality for independent refinement (squares) and difference refinement (triangles) of a variant struture for a simulated peptide of 51 atoms. The shift between the known native and variant structures was 0.1 /~; two unmodeiled water molecules were added at the same positions in native and variant structures. (a) The .m.s, errors in the model ariant atomic coordinates. (b) The r.m.s, errors in the displacements from model native to model variant structures.

Figure 3.
Fig. 3. The effects of decreasing the correlation in modeling errors. Conditions were the same as for Fig. 2 except hat the shift between the known native and variant structures was held fixed at 0.1 A r.m.s. while the two unmodelled water molecules were placed at different locations in the know native and variant structures.

The above figures are reproduced from the cited reference with permission from the IUCr

Secondary reference #2

Title

Structure of the gene V protein of bacteriophage f1 determined by multiwavelength X-Ray diffraction on the selenomethionyl protein.

Authors

M.M.Skinner, H.Zhang, D.H.Leschnitzer, Y.Guan, H.Bellamy, R.M.Sweet, C.W.Gray, R.N.Konings, A.H.Wang, T.C.Terwilliger.

Ref.

Proc Natl Acad Sci U S A, 1994, 91, 2071-2075. [DOI no: 10.1073/pnas.91.6.2071]

PubMed id

8134350