4W6V

Crystal structure of a peptide transporter from Yersinia enterocolitica at 3 A resolution

Summary for 4W6V

Entry DOI	10.2210/pdb4w6v/pdb
Descriptor	Di-/tripeptide transporter (1 entity in total)
Functional Keywords	membrane protein, transport protein, solute transporter, permease
Biological source	Yersinia enterocolitica subsp. palearctica YE-P4
Total number of polymer chains	1
Total formula weight	56509.90
Authors	Jeckelmann, J.-M.,Boggavarapu, R.,Harder, D.,Ucurum, Z.,Fotiadis, D. (deposition date: 2014-08-21, release date: 2015-07-15, Last modification date: 2024-01-10)
Primary citation	Boggavarapu, R.,Jeckelmann, J.M.,Harder, D.,Ucurum, Z.,Fotiadis, D. Role of electrostatic interactions for ligand recognition and specificity of peptide transporters. Bmc Biol., 13:58-58, 2015 Cited by PubMed Abstract: Peptide transporters are membrane proteins that mediate the cellular uptake of di- and tripeptides, and of peptidomimetic drugs such as β-lactam antibiotics, antiviral drugs and antineoplastic agents. In spite of their high physiological and pharmaceutical importance, the molecular recognition by these transporters of the amino acid side chains of short peptides and thus the mechanisms for substrate binding and specificity are far from being understood. PubMed: 26246134 DOI: 10.1186/s12915-015-0167-8 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3.01819 Å)

Structure validation