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1s0w
From Proteopedia
| 1s0w, resolution 2.30Å () | |
|---|---|
| Ligands: | |
| Domains: | PenP, BLIP |
| Related: | 1jtg |
| Resources: | FirstGlance, OCA, PDBsum, RCSB, TOPSAN |
| Coordinates: | save as pdb, mmCIF, xml |
TEM1-β-Lactamase/ β-Lactamase Inhibitor Protein (BLIP)
For additional information please see 2b5r
Protein-protein interactions are essential for life. Yet, our understanding of the general principles governing binding is not complete. In the present study, we show that the interface between proteins is built in a modular fashion; each module is comprised of a number of closely interacting residues, with few interactions between the modules. The boundaries between modules are defined by clustering the contact map of the interface. We show that mutations in one module do not affect residues located in a neighboring module. As a result, the structural and energetic consequences of the deletion of entire modules are surprisingly small. To the contrary, within their module, mutations cause complex energetic and structural consequences. Experimentally, this phenomenon is shown on the interaction between TEM1-beta-lactamase and beta-lactamase inhibitor protein (BLIP) by using multiple-mutant analysis and x-ray crystallography. Replacing an entire module of five interface residues with Ala created a large cavity in the interface, with no effect on the detailed structure of the remaining interface. The modular architecture of binding sites, which resembles human engineering design, greatly simplifies the design of new protein interactions and provides a feasible view of how these interactions evolved.
The modular architecture of protein-protein binding interfaces., Reichmann D, Rahat O, Albeck S, Meged R, Dym O, Schreiber G, Proc Natl Acad Sci U S A. 2005 Jan 4;102(1):57-62. Epub 2004 Dec 23. PMID:15618400
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
The enzyme TEM1 and its protein inhibitor, form the . BLIP(F142A) in complex with WT TEM1 (lime; 1s0w) in with the wildtype structure of the complex (magenta; 1jtg) and the two protein structures as determined in their unbound state (orange). Unbound TEM1 is structure 1btl; and unbound structure of BLIP is from ref. 2. T marks residues of TEM1 and B of BLIP. The distance between TEM Glu-104 and BLIP Lys-74 is marked for the wildtype and BLIP (F142A, 1s0w) complex structures.
About this Structure
1S0W is a Protein complex structure of sequences from Escherichia coli and Streptomyces clavuligerus. Full crystallographic information is available from OCA.
Reference
1) The modular architecture of protein-protein binding interfaces., Reichmann D, Rahat O, Albeck S, Meged R, Dym O, Schreiber G, Proc Natl Acad Sci U S A. 2005 Jan 4;102(1):57-62. Epub 2004 Dec 23. PMID:15618400
2) Structural and kinetic characterization of a beta-lactamase-inhibitor protein., Strynadka NC, Jensen S, Johns K, Blanchard H, Page M, Matagne A. et al., Nature 1994 Apr 14;368(6472):657-60. PMID: 8145854
Page seeded by OCA on Tue Jul 29 16:20:45 2008
Categories: Escherichia coli | Protein complex | Streptomyces clavuligerus | ISPC, Israel Structural Proteomics Center. | Reichman, D. | Schreiber, G. | Beta-lactamase inhibitor protein | Blip | ISPC | Israel Structural Proteomics Center | Protein-protein complex | Structural genomic | Tem-1 beta-lactamase
