5KF3

Truncated hemolysin A from P. mirabilis Y134A at 2.2 Angstroms resolution

Summary for 5KF3

• Entry DOI: 10.2210/pdb5kf3/pdb
• Related: 4w8q 5kdk 5keh
• Descriptor: Hemolysin (2 entities in total)
• Functional Keywords: hemolysin, two partner secretion, beta solenoid, beta helix, toxin
• Biological source: Proteus mirabilis
• Total number of polymer chains: 1
• Total formula weight: 25387.03

Authors

Novak, W.R.P.,Bhattacharyya, B.,Weaver, T.M. (deposition date: 2016-06-11, release date: 2017-03-22, Last modification date: 2024-10-16)

Primary citation

Novak, W.R.,Bhattacharyya, B.,Grilley, D.P.,Weaver, T.M.
Proteolysis of truncated hemolysin A yields a stable dimerization interface.
Acta Crystallogr F Struct Biol Commun, 73:138-145, 2017

PubMed Abstract: Wild-type and variant forms of HpmA265 (truncated hemolysin A) from Proteus mirabilis reveal a right-handed, parallel β-helix capped and flanked by segments of antiparallel β-strands. The low-salt crystal structures form a dimeric structure via the implementation of on-edge main-chain hydrogen bonds donated by residues 243-263 of adjacent monomers. Surprisingly, in the high-salt structures of two variants, Y134A and Q125A-Y134A, a new dimeric interface is formed via main-chain hydrogen bonds donated by residues 203-215 of adjacent monomers, and a previously unobserved tetramer is formed. In addition, an eight-stranded antiparallel β-sheet is formed from the flap regions of crystallographically related monomers in the high-salt structures. This new interface is possible owing to additional proteolysis of these variants after Tyr240. The interface formed in the high-salt crystal forms of hemolysin A variants may mimic the on-edge β-strand positioning used in template-assisted hemolytic activity.

PubMed: 28291749
DOI: 10.1107/S2053230X17002102

Experimental method

X-RAY DIFFRACTION (2.2 Å)