Structures of Brucella ovis leucine-, isoleucine-, valine-, threonine- and alanine-binding protein reveal a conformationally flexible peptide-binding cavity

Chakafana, G.; Boswell, R.; Chandler, A.; Jackson, K.A.; Neblett, S.; Postal, T.; Subramanian, S.; Abendroth, J.; Myler, P.J.; Asojo, O.A.

doi:10.1107/S2053230X24007027

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 1
BoLBP structure. (a) A ribbon diagram of BoLBP shows 15 β-sheets (purple) and 14 α-helices (cyan). (b) The BoLBP topology has two globular domains. α-Helices are labeled α, β-strands are labeled β and the three inter-domain loops are labeled L1, L2 and L3. (c) Superposed BoLBP structures. The orthorhombic monomer (blue) has a more open substrate binding cavity than the monoclinic monomer (gray).

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 80| Part 9| September 2024| Pages 193-199

https://doi.org/10.1107/S2053230X24007027

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