PDBsum entry: 1u11

Lyase

PDB id: 1u11

Contents

Protein chains

159 a.a. *

Ligands

CIT ×2

Waters ×262

* Residue conservation analysis

PDB id:

1u11

Name:

Lyase

Title:

Pure (n5-carboxyaminoimidazole ribonucleotide mutase) from t acidophile acetobacter aceti

Structure:

Pure (n5-carboxyaminoimidazole ribonucleotide mut chain: a, b. Engineered: yes

Source:

Acetobacter aceti. Organism_taxid: 435. Gene: pure. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Octamer (from PDB file)

Resolution:

1.55Å R-factor: 0.189 R-free: 0.199

Authors:

E.C.Settembre,J.R.Chittuluru,C.P.Mill,T.J.Kappock,S.E.Ealick

Key ref:

E.C.Settembre et al. (2004). Acidophilic adaptations in the structure of Acetobacter aceti N5-carboxyaminoimidazole ribonucleotide mutase (PurE). Acta Crystallogr D Biol Crystallogr, 60, 1753-1760. PubMed id: 15388921 DOI: 10.1107/S090744490401858X

Date:

14-Jul-04 Release date: 28-Sep-04

Protein chains

Q2QJL3  (Q2QJL3_ACEAC) -  N5-carboxyaminoimidazole ribonucleotide mutase

Seq: 182 a.a.

Struc: 159 a.a.

Enzyme reactions

• Enzyme class: E.C.5.4.99.18 - 5-(carboxyamino)imidazole ribonucleotide mutase.
• Reaction: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxylate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Biological process: purine nucleotide biosynthetic process (2 terms)
• Biochemical function: isomerase activity (3 terms)

Added reference

DOI no: 10.1107/S090744490401858X

Acta Crystallogr D Biol Crystallogr 60:1753-1760 (2004)

PubMed id: 15388921

Acidophilic adaptations in the structure of Acetobacter aceti N5-carboxyaminoimidazole ribonucleotide mutase (PurE).

E.C.Settembre, J.R.Chittuluru, C.P.Mill, T.J.Kappock, S.E.Ealick.

ABSTRACT

The crystal structure of Acetobacter aceti PurE was determined to a resolution of 1.55 A and is compared with the known structures of the class I PurEs from a mesophile, Escherichia coli, and a thermophile, Thermotoga maritima. Analyses of the general factors that increase protein stability are examined as potential explanations for the acid stability of A. aceti PurE. Increased inter-subunit hydrogen bonding and an increased number of arginine-containing salt bridges appear to account for the bulk of the increased acid stability. A chain of histidines linking two active sites is discussed in the context of the proton transfers catalyzed by the enzyme.

Selected figure(s)

Figure 2.
Figure 2 Electrostatic surface representation of AaPurE, EcPurE and TmPurE calculated with SPOCK (Christopher, 1998[106] [Christopher, J. A. (1998). Texas A&M University, College Station, Texas, USA.]-[107][bluearr.gif] ). Only protein atoms were considered in the calculation. The surface is colored blue for positively charged residues and red for negatively charged residues. The saturation of the color is proportional to the degree of electrostatic charge from -25kT to 25kT. (a) AaPurE is shown with citrate bound at the active sites. Citrate is colored green and drawn in ball-and-stick representation. (b) EcPurE is shown with AIR bound at the active site. AIR is colored green and drawn in ball-and-stick representation. (c) TmPurE in the same orientation as the other two PurEs.

Figure 5.
Figure 5 The chain of histidines linking two active sites are drawn in ball-and-stick representation and labeled with a prime to indicate donation from a neighboring subunit. A surface representation of the surrounding residues is shown with the opening created by cutting off one side of the channel. The coloring is based on charge from -25kT to 25kT. This figure was prepared with SPOCK (Christopher, 1998[168] [Christopher, J. A. (1998). Texas A&M University, College Station, Texas, USA.]-[169][bluearr.gif] ).

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2004, 60, 1753-1760) copyright 2004.

Figures were selected by an automated process.