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

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 2
ENDscript alignment reveals conserved residues between BoLBP and its closest structural neighbors. Identical and conserved residues are highlighted in red and yellow, respectively. The different secondary-structure elements shown are α-helices (α), 3₁₀-helices (η), β-strands (β) and β-turns (TT).

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

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

https://doi.org/10.1107/S2053230X24007027

Open

access

Follow Acta Cryst. F

Search IUCr Journals		doi		Advanced search
Author		volume	page