First time at Proteopedia? Click on the green links, they change the 3D image. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.
1xxm
From Proteopedia
| 1xxm, resolution 1.90Å () | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | bla (Escherichia coli) | ||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
| Domains: | PenP, BLIP | ||||||
| Related: | 1s0w | ||||||
| |||||||
| |||||||
| 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 . The TEM1–BLIP binding interface of the KFYEY mutant structure (1xxm), on the wildtype complex (1jtg) interface. Mutated TEM1 and BLIP (1xxm) are colored in red and lime, respectively, while wildtype TEM1 and BLIP (1jtg) are colored in yellow and orange, respectively. Mutated BLIP residues (K74A, F142A, Y143A) are colored in blue-violet and TEM1 mutated residues E104A and Y105A are colored blue or magenta in the multiple mutant complex (KFYEY). These two structures are very similar, except for the deletion of the five mutated side-chains. All-atom RMS deviation (RMSD) between the interfaces of the wildtype and the KFYEY mutant structures is 0.37 Å.
About this Structure
1XXM is a Protein complex structure of sequences from Escherichia coli and Streptomyces clavuligerus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Jul 27 20:59:12 2008
Categories: Beta-lactamase | Escherichia coli | Protein complex | Streptomyces clavuligerus | Albeck, S. | Dym, O. | ISPC, Israel Structural Proteomics Center. | Meged, R. | Rahat, O. | Reichmann, D. | Schreiber, G. | Beta-2 lactamase inhibitor protein | Blip | ISPC | Israel Structural Proteomics Center | Protein-protein complex | Structural genomic | Tem-1 beta-lactamase
