Co-crystal structure of Helicobacter pylori biotin protein ligase with biotinyl-5-ATP

Ayanlade, J.P.; Davis, D.E.; Subramanian, S.; Dranow, D.M.; Lorimer, D.D.; Hammerson, B.; Myler, P.J.; Asojo, O.A.

doi:10.1107/S2053230X24012056

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 3
(a) The solvent-accessible surface area of HpBPL is colored by sequence conservation, with red indicating identical residues. (b) Ribbon diagram calculated by ENDScript. The circumference of the ribbon (sausage) represents relative structural conservation compared with other BPL structures. Thinner ribbons represent more conserved regions. In comparison, thicker ribbons represent less conserved regions and the ribbon is colored by sequence conservation, with red indicating identical residues. (c) Alignment of HpBPL and MtBPL. The PDB entries of the protein structures used for this alignment are indicated in Supplementary Fig. S1.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 81| Part 1| January 2025|

https://doi.org/10.1107/S2053230X24012056

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