1k67

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

MODEL INTERACTION BETWEEN BIRA AND BCCP

spinqualitylabelsall models 1k67 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed A model is suggested for the complex between the biotin repressor of Escherichia coli, BirA, and BCCP, the biotin carboxyl carrier protein to which BirA transfers biotin. The model is consistent with prior physical and biochemical studies. Measurement of transfer rates for variants of BirA with single-site mutations in the proposed BirA:BCCP interface region also provides support. The unique feature of the proposed interaction between BirA and BCCP is that it uses the same beta-sheet region on the surface of BirA that the protein uses for homodimerization into a form competent to bind DNA. The resulting mutually exclusive protein:protein interfaces explain the novel feature of the BirA regulatory system, namely, that transcription of the genes involved in biotin synthesis is not determined by the level of biotin, per se, but by the level of unmodified BCCP. The model also provides a role for the C-terminal domain of BirA that is structurally similar to an SH3 domain. Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor.,Weaver LH, Kwon K, Beckett D, Matthews BW Protein Sci. 2001 Dec;10(12):2618-22. PMID:11714930 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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