4PK0: Crystal Structure Of T4 Lysozyme-peptide In Complex With Teicoplanin- A2-2

Citation:
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 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.
PDB ID: 4PK0Download
MMDB ID: 123040
PDB Deposition Date: 2014/5/13
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
Similar Structures:
Biological Unit for 4PK0: dimeric; determined by author
Molecular Components in 4PK0
Label Count Molecule
Protein (1 molecule)
1
Lysozyme
Molecule annotation
Nucleotide(1 molecule)
1
Teicoplanin-a2-2
Molecule annotation
Chemicals (8 molecules)
1
1
2
1
3
1
4
1
5
1
6
1
7
1
8
1
* Click molecule labels to explore molecular sequence information.

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