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1btl
From Proteopedia
| 1btl, resolution 1.80Å () | |||||||||
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| Ligands: | |||||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||||
| Domains: | PenP | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
CRYSTAL STRUCTURE OF ESCHERICHIA COLI TEM1 BETA-LACTAMASE AT 1.8 ANGSTROMS RESOLUTION
(see also page TEM1-beta-Lactamase/beta-lactamase Inhibitor Protein (BLIP))
The X-ray structure of Escherichia coli TEM1 beta-lactamase has been refined to a crystallographic R-factor of 16.4% for 22,510 reflections between 5.0 and 1.8 A resolution; 199 water molecules and 1 sulphate ion were included in refinement. Except for the tips of a few solvent-exposed side chains, all protein atoms have clear electron density and refined to an average atomic temperature factor of 11 A2. The estimated coordinates error is 0.17 A. The substrate binding site is located at the interface of the two domains of the protein and contains 4 water molecules and the sulphate anion. One of these solvent molecules is found at hydrogen bond distance from S70 and E166. S70 and S130 are hydrogen bonded to K73 and K234, respectively. It was found that the E. coli TEM1 and Staphylococcus aureus PC1 beta-lactamases crystal structures differ in the relative orientations of the two domains composing the enzymes, which result in a narrowed substrate binding cavity in the TEM1 enzyme. Local but significant differences in the vicinity of this site may explain the occurrence of TEM1 natural mutants with extended substrate specificities.
Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution., Jelsch C, Mourey L, Masson JM, Samama JP, Proteins. 1993 Aug;16(4):364-83. PMID:8356032
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
The enzyme TEM1 β-lactamase (EC 3.5.2.6; and its protein inhibitor, form a . of the residues which participate in TEM1-BLIP interactions between: 1) complex of mutated BLIP (F142A) and wildtype TEM1 (lime; 1s0w); 2) complex of the wildtype BLIP/wildtype TEM1 (magenta; 1jtg); 3) unbound wildtype BLIP (structure from Ref 2) and unbound wildtype TEM1 (1btl), these two structures colored orange). T marks residues of TEM1 and B of BLIP. The distance between TEM Glu-104 and BLIP Lys-74 is marked for the wildtype (1jtg) and mutated (F142A, 1s0w) TEM1-BLIP complex structures.
The complex where BLIP residues of the bound structure are colored blue and of the unbound are in cyan. TEM1 residues from the bound complex are in red and from the unbound structure in yellow. BLIP and TEM1 residues are labeled blue and red. The between BLIP and TEM1 was divided into six interface clusters (, , , , , , 2b5r). Superpositions of these clusters from TEM1–BLIP (complex-1jtg), TEM1 (unbound-1btl) and BLIP (unbound, from Ref 2) structures are shown. of cluster C1 from TEM1-BLIP wt, mutant and unbound structures (TEM1wt-BLIPwt complex, TEM1wt-BLIPD49A, unbound TEM1 (yellow), and unbound BLIP). D49 in BLIP is located in the center of C1, surrounded by 4 TEM1 residues. The D49A mutation (i.e. removal of a side chain) does not cause structural change in the TEM1-BLIP complex.
About this Structure
1BTL is a 1 chain structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
References
- Jelsch C, Mourey L, Masson JM, Samama JP. Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution. Proteins. 1993 Aug;16(4):364-83. PMID:8356032 doi:10.1002/prot.340160406
- Strynadka NC, Jensen SE, Johns K, Blanchard H, Page M, Matagne A, Frere JM, James MN. Structural and kinetic characterization of a beta-lactamase-inhibitor protein. Nature. 1994 Apr 14;368(6472):657-60. PMID:8145854 doi:10.1038/368657a0
- Reichmann D, Cohen M, Abramovich R, Dym O, Lim D, Strynadka NC, Schreiber G. Binding hot spots in the TEM1-BLIP interface in light of its modular architecture. J Mol Biol. 2007 Jan 19;365(3):663-79. Epub 2006 Oct 3. PMID:17070843 doi:10.1016/j.jmb.2006.09.076
Page seeded by OCA on Tue Feb 17 20:15:07 2009
