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1xxm
From Proteopedia
| 1xxm, resolution 1.90Å () | |||||||||
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| Ligands: | |||||||||
| Gene: | bla (Escherichia coli) | ||||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||||
| Domains: | PenP, BLIP | ||||||||
| Related: | 1s0w | ||||||||
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| 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 a . The TEM1–BLIP in the KFYEY mutant structure (1xxm) is on the wildtype complex (1jtg) structure. Mutated TEM1 is shown in red, BLIP (lime) (1xxm) , wildtype TEM1 (yellow) and BLIP (1jtg) in orange, respectively. Mutated BLIP residues (K74A, F142A, Y143A) are colored in blue-violet, TEM1 residues E104 and Y105, where mutations to alanines were performed (i.g. E104A, Y105A), are colored blue and corresponding to them alanines A104 and A105 are colored magenta in the multiple mutant complex (KFYEY). These two structures are very similar. All-atom RMS deviation (RMSD) between the structures of the wildtype and the KFYEY mutant 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
Proteopedia Page Contributors and Editors (what is this?)
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
