PDBsum entry 1pvs

Hydrolase

PDB id

1pvs

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Contents

			Protein chains

					282 a.a. *

			Ligands

					7HP ×2

			Waters ×226

* Residue conservation analysis

PDB id:

1pvs

Links
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Name:

Hydrolase

Title:

3-methyladenine glcosylase ii(alka) hypoxanthine complex

Structure:

DNA-3-methyladenine glycosylase ii. Chain: a, b. Synonym: 3-methyladenine-DNA glycosylase ii, inducible, tag ii, DNA- 3-methyladenine glycosidase ii. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Gene: alka or aida or b2068. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.40Å

R-factor:

0.232

R-free:

0.292

Authors:

M.Teale

Key ref:

M.Teale et al. (2002). 3-methyladenine-DNA glycosylase II: the crystal structure of an AlkA-hypoxanthine complex suggests the possibility of product inhibition. Bioconjug Chem, 13, 403-407. PubMed id: 12009927

Date:

28-Jun-03

Release date:

08-Jun-04

PROCHECK

	Headers

	References

Protein chains

P04395 (3MG2_ECOLI) - DNA-3-methyladenine glycosylase 2 from Escherichia coli (strain K12)

Seq: Struc:					282 a.a. 282 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.3.2.2.21 - DNA-3-methyladenine glycosylase Ii.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine, and 7-methyladenine.

	Bioconjug Chem 13:403-407 (2002)
PubMed id: 12009927

3-methyladenine-DNA glycosylase II: the crystal structure of an AlkA-hypoxanthine complex suggests the possibility of product inhibition.
M.Teale, J.Symersky, L.DeLucas.

ABSTRACT

Escherichia coli (E. coli) protein 3-methyladenine-DNA glycosylase II (AlkA) functions primarily by removing alkylation damage from duplex and single stranded DNA. A crystal structure of AlkA was refined to 2.0 A resolution. This structure in turn was used to refine an AlkA-hypoxanthine (substrate) complex structure to 2.4 A resolution. The complex structure shows hypoxanthine located in AlkA's active site stacked between residues W218 and Y239. The structural analysis of the AlkA and AlkA-hypoxanthine structures indicate that free hypoxanthine binding in the active site may inhibit glycosylase activity.

Literature references that cite this PDB file's key reference

PubMed id

Reference

18472311

G.M.Lingaraju, M.Kartalou, L.B.Meira, and L.D.Samson (2008).
Substrate specificity and sequence-dependent activity of the Saccharomyces cerevisiae 3-methyladenine DNA glycosylase (Mag).

DNA Repair (Amst), 7, 970-982.

18464997

L.R.Rutledge, H.F.Durst, and S.D.Wetmore (2008).
Computational comparison of the stacking interactions between the aromatic amino acids and the natural or (cationic) methylated nucleobases.

Phys Chem Chem Phys, 10, 2801-2812.

18464978

P.Cysewski (2008).
A post-SCF complete basis set study on the recognition patterns of uracil and cytosine by aromatic and pi-aromatic stacking interactions with amino acid residues.

Phys Chem Chem Phys, 10, 2636-2645.

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.