4PK0

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

Summary for 4PK0

• Entry DOI: 10.2210/pdb4pk0/pdb
• Related: 4PJZ
• Related PRD ID: PRD_002089
• Descriptor: TEICOPLANIN-A2-2, GLYCEROL, Lysozyme, ... (11 entities in total)
• Functional Keywords: site-selective catalyst, carrier protein approach, glycopeptide antibiotic, hydrolase-antibiotic complex, hydrolase/antibiotic
• Biological source: Enterobacteria phage T4; More
• Total number of polymer chains: 2
• Total formula weight: 21541.46

Authors

Han, S.,Le, B.V.,Hajare, H.,Baxter, R.H.G.,Miller, S.J. (deposition date: 2014-05-13, release date: 2014-09-10, Last modification date: 2023-12-27)

Primary citation

Han, S.,Le, B.V.,Hajare, H.S.,Baxter, R.H.,Miller, S.J.
X-ray Crystal Structure of Teicoplanin A2-2 Bound to a Catalytic Peptide Sequence via the Carrier Protein Strategy.
J.Org.Chem., 79:8550-8556, 2014

PubMed Abstract: 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 Å 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 Å) to the N-acetylglucosamine than the two other sugar rings present in teicoplanin (9.3 and 20.3 Å, 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.

PubMed: 25147913
DOI: 10.1021/jo501625f

Experimental method

X-RAY DIFFRACTION (2.3 Å)