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4N13

Crystal Structure of PstS (BB_0215) from Borrelia burgdorferi

Summary for 4N13
Entry DOI10.2210/pdb4n13/pdb
DescriptorPhosphate ABC transporter, periplasmic phosphate-binding protein, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywordsclass ii ligand-binding protein, ligand-binding protein, phosphate-binding protein, abc transporter, transport protein
Biological sourceBorrelia burgdorferi
Total number of polymer chains1
Total formula weight29788.33
Authors
Brautigam, C.A.,Deka, R.K.,Norgard, M.V. (deposition date: 2013-10-03, release date: 2014-01-22, Last modification date: 2023-09-20)
Primary citationBrautigam, C.A.,Ouyang, Z.,Deka, R.K.,Norgard, M.V.
Sequence, biophysical, and structural analyses of the PstS lipoprotein (BB0215) from Borrelia burgdorferi reveal a likely binding component of an ABC-type phosphate transporter.
Protein Sci., 23:200-212, 2014
Cited by
PubMed Abstract: The Lyme disease agent Borrelia burgdorferi, which is transmitted via a tick vector, is dependent on its tick and mammalian hosts for a number of essential nutrients. Like other bacterial diderms, it must transport these biochemicals from the extracellular milieu across two membranes, ultimately to the B. burgdorferi cytoplasm. In the current study, we established that a gene cluster comprising genes bb0215 through bb0218 is cotranscribed and is therefore an operon. Sequence analysis of these proteins suggested that they are the components of an ABC-type transporter responsible for translocating phosphate anions from the B. burgdorferi periplasm to the cytoplasm. Biophysical experiments established that the putative ligand-binding protein of this system, BbPstS (BB0215), binds to phosphate in solution. We determined the high-resolution (1.3 Å) crystal structure of the protein in the absence of phosphate, revealing that the protein's fold is similar to other phosphate-binding proteins, and residues that are implicated in phosphate binding in other such proteins are conserved in BbPstS. Taken together, the gene products of bb0215-0218 function as a phosphate transporter for B. burgdorferi.
PubMed: 24318969
DOI: 10.1002/pro.2406
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.3 Å)
Structure validation

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