2y3e

TRAPTAVIDIN, APO-FORM

spinqualitylabelsall models 2y3e, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2y3e is a 2 chain structure with sequence from Streptomyces avidinii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL Related: 1swh, 2bc3, 1vwq, 1swf, 1sre, 1lcw, 2rtb, 1swp, 1hxz, 1rxj, 1swe, 1mm9, 2rtr, 1swa, 2rto, 2rtd, 1stp, 1n43, 1sri, 2izh, 1slf, 1swc, 1vwr, 1swl, 1ndj, 1str, 1vwm, 1slg, 1swd, 1swq, 1swu, 1i9h, 2rtj, 1swj, 2rtl, 2iza, 1vwk, 1vwn, 1vwg, 1moy, 1sts, 1hqq, 1vwi, 2izg, 2izb, 1swg, 1luq, 1swk, 2izk, 2y3f, 1sws, 1n4j, 2izd, 1swt, 1lcv, 1df8, 1vwl, 2wpu, 1vwb, 1srj, 2rtk, 1kl3, 2rti, 2izf, 1swr, 2rth, 2rtm, 2izi, 1vwf, 1vwh, 1pts, 1mk5, 1hxl, 2f01, 1vwd, 1nc9, 1sle, 1vwj, 2ize, 2rtf, 2rtp, 1n9y, 1n9m, 1lcz, 1nqm, 1hy2, 1vwa, 2izl, 2izc, 1kl5, 1mep, 1sld, 1rxh, 1rsu, 1vwc, 1nbx, 2izj, 1srh, 1rst, 1kff, 1srg, 1vwe, 2rtg, 1srf, 1kl4, 1rxk, 2rtq, 1vwo, 1swb, 2rte, 2rta, 2rtc, 1swo, 2rtn, 1swn, 1n7y, 1vwp Resources: FirstGlance, OCA, RCSB, PDBsum Function [SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). Publication Abstract from PubMed The interaction between streptavidin and biotin is one of the strongest non-covalent interactions in nature. Streptavidin is a widely used tool and a paradigm for protein-ligand interactions. We recently developed a streptavidin mutant, termed traptavidin, possessing 10-fold lower off-rate for biotin, with increased mechanical and thermal stability. Here, we determined crystal structures of apo-traptavidin and biotin-traptavidin at 1.5 A resolution. In apo-streptavidin the L3/4 loop, near biotin's valeryl tail, is typically disordered and open, but closes upon biotin binding. In contrast, this L3/4 loop was shut in both apo-traptavidin and biotin-traptavidin. The reduced flexibility of L3/4 and decreased conformational change on biotin binding provide an explanation for traptavidin's reduced biotin off-rate and on-rate. The L3/4 loop includes Ser-45, which forms a hydrogen bond to biotin consistently in traptavidin but erratically in streptavidin. Reduced breakage of the biotin:Ser-45 hydrogen bond in traptavidin is likely to inhibit the initiating event in biotin's dissociation pathway. We generated a traptavidin with 1 biotin binding site rather than 4, which showed a similarly slow off-rate, demonstrating that traptavidin's slow off-rate was governed by intra-subunit effects. Understanding the structural features of this tenacious interaction may assist design of even stronger affinity tags and inhibitors. How the biotin-streptavidin interaction was made even stronger: investigation via crystallography and a chimeric tetramer.,Chivers CE, Koner AL, Lowe ED, Howarth M Biochem J. 2011 Jan 18. PMID:21241253 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Avidin

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