4pk0 | pdb_00004pk0

CRYSTAL STRUCTURE OF T4 LYSOZYME-PEPTIDE IN COMPLEX WITH TEICOPLANIN-A2-2

spinqualitylabelsall models 4pk0, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pk0 is a 2 chain structure with sequence from Actinoplanes teichomyceticus and Escherichia virus T4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: 3FG, 3MY, AIB, CCS, CL, DAL, DPR, GCS, GHP, GOL, MAN, MHS, NA, NAG, OMY, PO4, PRD_002089, T55 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D9IEF7_BPT4 Publication Abstract from PubMed We report the X-ray crystal structure of a site-selective peptide catalyst moiety and teicoplanin A2-2 complex. The expressed protein ligation technique was used to couple T4 lysozyme (T4L) and a synthetic peptide catalyst responsible for the selective phosphorylation of the N-acetylglucosamine sugar in a teicoplanin A2-2 derivative. The T4L-Pmh-dPro-Aib-dAla-dAla construct was crystallized in the presence of teicoplanin A2-2. The resulting 2.3 A resolution protein-peptide-teicoplanin complex crystal structure revealed that the nucleophilic nitrogen of N-methylimidazole in the Pmh residue is in closer proximity (7.6 A) to the N-acetylglucosamine than the two other sugar rings present in teicoplanin (9.3 and 20.3 A, respectively). This molecular arrangement is consistent with the observed selectivity afforded by the peptide-based catalyst when it is applied to a site-selective phosphorylation reaction involving a teicoplanin A2-2 derivative. X-ray Crystal Structure of Teicoplanin A-2 Bound to a Catalytic Peptide Sequence via the Carrier Protein Strategy.,Han S, Le BV, Hajare HS, Baxter RH, Miller SJ J Org Chem. 2014 Sep 2. PMID:25147913 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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