3TPA

Structure of HbpA2 from Haemophilus parasuis

Summary for 3TPA

• Entry DOI: 10.2210/pdb3tpa/pdb
• Descriptor: Heme-binding protein A (2 entities in total)
• Functional Keywords: glutathione binding protein, heme binding protein, sbp
• Biological source: Haemophilus parasuis 29755
• Total number of polymer chains: 1
• Total formula weight: 58883.92

Authors

Vergauwen, B.,Van der Meeren, R.,Dansercoer, A.,Savvides, S.N. (deposition date: 2011-09-07, release date: 2011-11-30, Last modification date: 2024-11-20)

Primary citation

Vergauwen, B.,Van der Meeren, R.,Dansercoer, A.,Savvides, S.N.
Delineation of the Pasteurellaceae-specific GbpA-family of glutathione-binding proteins.
Bmc Biochem., 12:59-59, 2011

PubMed Abstract: The Gram-negative bacterium Haemophilus influenzae is a glutathione auxotroph and acquires the redox-active tripeptide by import. The dedicated glutathione transporter belongs to the ATP-binding cassette (ABC)-transporter superfamily and displays more than 60% overall sequence identity with the well-studied dipeptide (Dpp) permease of Escherichia coli. The solute binding protein (SBP) that mediates glutathione transport in H. influenzae is a lipoprotein termed GbpA and is 54% identical to E. coli DppA, a well-studied member of family 5 SBP's. The discovery linking GbpA to glutathione import came rather unexpectedly as this import-priming SBP was previously annotated as a heme-binding protein (HbpA), and was thought to mediate heme acquisition. Nonetheless, although many SBP's have been implicated in more than one function, a prominent physiological role for GbpA and its partner permease in heme acquisition appears to be very unlikely. Here, we sought to characterize five representative GbpA homologs in an effort to delineate the novel GbpA-family of glutathione-specific family 5 SBPs and to further clarify their functional role in terms of ligand preferences.

PubMed: 22087650
DOI: 10.1186/1471-2091-12-59

Experimental method

X-RAY DIFFRACTION (2.0001 Å)