PDBsum entry 3dff

Hydrolase

PDB id

3dff

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Contents

			Protein chain

					266 a.a. *

			Ligands

					PG4


					GOL

			Metals

					_ZN

			Waters ×241

* Residue conservation analysis

PDB id:

3dff

Links

Name:

Hydrolase

Title:

The crystal structure of teicoplanin pseudoaglycone deacetylase orf2

Structure:

Teicoplanin pseudoaglycone deacetylases orf2. Chain: a. Engineered: yes

Source:

Actinoplanes teichomyceticus. Organism_taxid: 1867. Gene: tcp14. Expressed in: escherichia coli

Resolution:

1.60Å

R-factor:

0.196

R-free:

0.223

Authors:

Y.Zou,J.S.Brunzelle,S.K.Nair

Key ref:

Y.Zou et al. (2008). Crystal structures of lipoglycopeptide antibiotic deacetylases: implications for the biosynthesis of A40926 and teicoplanin. Chem Biol, 15, 533-545. PubMed id: 18559264

Date:

11-Jun-08

Release date:

22-Jul-08

PROCHECK

	Headers

	References

Protein chain

Q6ZZJ1 (Q6ZZJ1_ACTTI) - LmbE family N-acetylglucosaminyl deacetylase from Actinoplanes teichomyceticus

Seq: Struc:					273 a.a. 266 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

	Chem Biol 15:533-545 (2008)
PubMed id: 18559264

Crystal structures of lipoglycopeptide antibiotic deacetylases: implications for the biosynthesis of A40926 and teicoplanin.
Y.Zou, J.S.Brunzelle, S.K.Nair.

ABSTRACT

The lipoglycopeptide antibiotics teicoplanin and A40926 have proven efficacy against Gram-positive pathogens. These drugs are distinguished from glycopeptide antibiotics by N-linked long chain acyl-D-glucosamine decorations that contribute to antibacterial efficacy. During the biosynthesis of lipoglycopeptides, tailoring glycosyltransferases attach an N-acetyl-D-glucosamine to the aglycone, and this N-acetyl-glucosaminyl pseudoaglycone is deacetylated prior to long chain hydrocarbon attachment. Here we present several high-resolution crystal structures of the pseudoaglycone deacetylases from the biosynthetic pathways of teicoplanin and A40926. The cocrystal structure of the teicoplanin pseudoaglycone deacetylase with a fatty acid product provides further insights into the roles of active-site residues, and suggests mechanistic similarities with structurally distinct zinc deacetylases, such as peptidoglycan deacetylase and LpxC. A unique, structurally mobile capping lid, located at the apex of these pseudoaglycone deacetylases, likely serves as a determinant of substrate specificity.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21267472

H.C.Chan, Y.T.Huang, S.Y.Lyu, C.J.Huang, Y.S.Li, Y.C.Liu, C.C.Chou, M.D.Tsai, and T.L.Li (2011).
Regioselective deacetylation based on teicoplanin-complexed Orf2* crystal structures.

Mol Biosyst, 7, 1224-1231.

PDB codes:

2x9l 2xad

20491912

A.Deli, D.Koutsioulis, V.E.Fadouloglou, P.Spiliotopoulou, S.Balomenou, S.Arnaouteli, M.Tzanodaskalaki, K.Mavromatis, M.Kokkinidis, and V.Bouriotis (2010).
LmbE proteins from Bacillus cereus are de-N-acetylases with broad substrate specificity and are highly similar to proteins in Bacillus anthracis.

FEBS J, 277, 2740-2753.

20414653

M.Sosio, A.Canavesi, S.Stinchi, and S.Donadio (2010).
Improved production of A40926 by Nonomuraea sp. through deletion of a pathway-specific acetyltransferase.

Appl Microbiol Biotechnol, 87, 1633-1638.

20970210

S.Jovetic, Y.Zhu, G.L.Marcone, F.Marinelli, and J.Tramper (2010).
β-Lactam and glycopeptide antibiotics: first and last line of defense?

Trends Biotechnol, 28, 596-604.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.