2J5Y

Crystal structure of the GA module from F.magna

Summary for 2J5Y

• Entry DOI: 10.2210/pdb2j5y/pdb
• Related: 1GAB 1PRB 1TF0
• Descriptor: PEPTOSTREPTOCOCCAL ALBUMIN-BINDING PROTEIN (2 entities in total)
• Functional Keywords: protein binding, cell wall, peptidoglycan-anchor, protein binding bacterial albumin-binding three-helix bundle
• Biological source: PEPTOSTREPTOCOCCUS MAGNUS
• Cellular location: Secreted, cell wall; Peptidoglycan-anchor (Potential): Q51911
• Total number of polymer chains: 2
• Total formula weight: 13639.71

Authors

Lejon, S.,Cramer, J.F.,Nordberg, P.A.,Lundqvist, T.,Valegard, K. (deposition date: 2006-09-20, release date: 2007-06-26, Last modification date: 2023-12-13)

Primary citation

Cramer, J.F.,Nordberg, P.A.,Hajdu, J.,Lejon, S.
Crystal Structure of a Bacterial Albumin-Binding Domain at 1.4A Resolution.
FEBS Lett., 581:3178-, 2007

PubMed Abstract: The albumin-binding domain, or GA module, of the peptostreptococcal albumin-binding protein expressed in pathogenic strains of Finegoldia magna is believed to be responsible for the virulence and increased growth rate of these strains. Here we present the 1.4A crystal structure of this domain, and compare it with the crystal structure of the GA-albumin complex. An analysis of protein-protein interactions in the two crystals, and the presence of multimeric GA species in solution, indicate the GA module is "sticky", and is capable of forming contacts with a range of protein surfaces. This might lead to interactions with different host proteins.

PubMed: 17575979
DOI: 10.1016/J.FEBSLET.2007.06.003

Experimental method

X-RAY DIFFRACTION (1.4 Å)