File:3-s2.0-B9780123786302000050-gr3.jpg
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Summary
| Description |
English: Three-dimensional structures of two biotin domains. The structures of the biotin domains from the biotin carboxyl carrier protein (BCCP) of (left) Escherichia coli acetyl CoA carboxylase and (right) the 1.3S subunit of Propionibacterium freudenreichii subsp. shermanii transcarboxylase (TC) have been determined. The holo forms of the two proteins with the biotin moiety specifically attached to the target lysine residues at position 122 and 89, respectively, are depicted. Solid arrows represent the β-strands in the fold. The amino (N) and carboxyl (C) termini of the domain are indicated. The molecules have been orientated to highlight the interaction of biotin with the thumb structure in BCCP. |
| Date | |
| Source | Lennarz, William J., and M. Daniel Lane. Encyclopedia of Biological Chemistry. Elsevier, 2013. |
| Author | William J. Lennarz |
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 18:53, 26 April 2023 | | 479 × 463 (37 KB) | Trivas47 | Uploaded a work by William J. Lennarz from Lennarz, William J., and M. Daniel Lane. Encyclopedia of Biological Chemistry. Elsevier, 2013. with UploadWizard |
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