4z2o | pdb_00004z2o

High resolution crystal structure of short hoefavidin-hoef-peptide complex

spinqualitylabelsall models 4z2o, resolution 1.17Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4z2o is a 2 chain structure with sequence from Hoeflea phototrophica DFL-43. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.17Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HOAVI_HOEPD The exact role played by hoefavidin in the host organism is still obscure. Forms a strong non-covalent complex with biotin and 2-iminobiotin. Publication Abstract from PubMed Dimeric avidins are a newly discovered subgroup of the avidin family that bind biotin with high affinity. Their dimeric configuration is a quaternary substructure of the classical tetrameric avidins which lacks the requirement of the critical Trp that defines the tetramer and dictates the tenacious interaction with biotin. Hoefavidin, derived from the bacterium Hoeflea phototrophica DFL-43T, is the third characterized member of the dimeric avidin subfamily. Like the other members of this group, hoefavidin is a thermostable protein that contains a disulfide bridge between Cys57 and Cys88, thereby connecting and stabilizing the L3,4 and L5,6 loops. This represents a distinctive characteristic of dimeric avidins that compensates for the lack of Trp and enables their dimeric configuration. The X-ray structure of the intact hoefavidin revealed unique crystal packing generated by an octameric cylindrical structure wherein the C-termini segments of each monomer is introduced into the entrance of the biotin-binding site of an adjacent non-canonical monomer. This anomaly in the protein structure served as a lead toward the design of specific binding peptides. We screened for specific hoefavidin binding peptides derived from the C-terminal region and two peptides were obtained that bind a truncated form of hoefavidin (lacking the last 10 amino acids) with dissociation constants of 10-5M. The crystal structure of short hoefavidin complexed with a C-terminal derived peptide revealed the mode of binding. These peptides may form the basis of novel and reversible binders for dimeric avidins. Hoefavidin: A dimeric bacterial avidin with a C-terminal binding tail.,Avraham O, Meir A, Fish A, Bayer EA, Livnah O J Struct Biol. 2015 Jun 27. pii: S1047-8477(15)30024-1. doi:, 10.1016/j.jsb.2015.06.020. PMID:26126731 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Avidin 3D structures

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