Crystal structure of a purine/pyrimidine phosphoribosyltransferase-related protein from Thermus thermophilus HB8

Peter H. Rehse, Tahir H Tahirov

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Adenine phosphoribosyltransferase (APRTase) is a widely distributed enzyme involved in the salvage of adenine to form an adenine nucleotide. We crystallized and determined the X-ray crystallographic structure of a purine/pyrimidine phosphoribosyltransferase-related protein from the thermophilic bacterium, Thermus thermophilus HB8. The crystal space group was C2 with unit cell dimensions of a = 167.42 Å, b = 61.41 Å, c = 102.39 Å, β = 94.0°. Initial phases were determined to 2.6 Å using the multiple wavelength anomalous dispersion method and selenomethionine substituted protein (Se-MAD), and refined using a 1.9 Å "native" data set. The asymmetric unit contains two pairs of identical dinners, each related by noncrystallographic two-fold symmetry. The fifth monomer forms a similar dinner across a crystallographic two-fold axis. These dimers appear to be the biological unit with both monomers contributing to an unusual highly charged arginine-rich bridge region separating the two active sites. Comparison with distantly related APRTases reveal similarities and differences of the active site.

Original languageEnglish (US)
Pages (from-to)658-665
Number of pages8
JournalProteins: Structure, Function and Genetics
Volume61
Issue number3
DOIs
StatePublished - Nov 15 2005

Fingerprint

Thermus thermophilus
Meals
Catalytic Domain
Adenine Phosphoribosyltransferase
Monomers
Crystal structure
Selenomethionine
Salvaging
Adenine Nucleotides
Adenine
Dimers
Arginine
Bacteria
Proteins
X-Rays
X rays
Wavelength
Crystals
Enzymes
pyrimidine phosphoribosyltransferase

Keywords

  • Adenosine phosphoribosyltransferase
  • X-ray

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

Cite this

Crystal structure of a purine/pyrimidine phosphoribosyltransferase-related protein from Thermus thermophilus HB8. / Rehse, Peter H.; Tahirov, Tahir H.

In: Proteins: Structure, Function and Genetics, Vol. 61, No. 3, 15.11.2005, p. 658-665.

Research output: Contribution to journalArticle

@article{7adfa51e0f9c4accbdccc7a594f03784,
title = "Crystal structure of a purine/pyrimidine phosphoribosyltransferase-related protein from Thermus thermophilus HB8",
abstract = "Adenine phosphoribosyltransferase (APRTase) is a widely distributed enzyme involved in the salvage of adenine to form an adenine nucleotide. We crystallized and determined the X-ray crystallographic structure of a purine/pyrimidine phosphoribosyltransferase-related protein from the thermophilic bacterium, Thermus thermophilus HB8. The crystal space group was C2 with unit cell dimensions of a = 167.42 {\AA}, b = 61.41 {\AA}, c = 102.39 {\AA}, β = 94.0°. Initial phases were determined to 2.6 {\AA} using the multiple wavelength anomalous dispersion method and selenomethionine substituted protein (Se-MAD), and refined using a 1.9 {\AA} {"}native{"} data set. The asymmetric unit contains two pairs of identical dinners, each related by noncrystallographic two-fold symmetry. The fifth monomer forms a similar dinner across a crystallographic two-fold axis. These dimers appear to be the biological unit with both monomers contributing to an unusual highly charged arginine-rich bridge region separating the two active sites. Comparison with distantly related APRTases reveal similarities and differences of the active site.",
keywords = "Adenosine phosphoribosyltransferase, X-ray",
author = "Rehse, {Peter H.} and Tahirov, {Tahir H}",
year = "2005",
month = "11",
day = "15",
doi = "10.1002/prot.20624",
language = "English (US)",
volume = "61",
pages = "658--665",
journal = "Proteins: Structure, Function and Bioinformatics",
issn = "0887-3585",
publisher = "Wiley-Liss Inc.",
number = "3",

}

TY - JOUR

T1 - Crystal structure of a purine/pyrimidine phosphoribosyltransferase-related protein from Thermus thermophilus HB8

AU - Rehse, Peter H.

AU - Tahirov, Tahir H

PY - 2005/11/15

Y1 - 2005/11/15

N2 - Adenine phosphoribosyltransferase (APRTase) is a widely distributed enzyme involved in the salvage of adenine to form an adenine nucleotide. We crystallized and determined the X-ray crystallographic structure of a purine/pyrimidine phosphoribosyltransferase-related protein from the thermophilic bacterium, Thermus thermophilus HB8. The crystal space group was C2 with unit cell dimensions of a = 167.42 Å, b = 61.41 Å, c = 102.39 Å, β = 94.0°. Initial phases were determined to 2.6 Å using the multiple wavelength anomalous dispersion method and selenomethionine substituted protein (Se-MAD), and refined using a 1.9 Å "native" data set. The asymmetric unit contains two pairs of identical dinners, each related by noncrystallographic two-fold symmetry. The fifth monomer forms a similar dinner across a crystallographic two-fold axis. These dimers appear to be the biological unit with both monomers contributing to an unusual highly charged arginine-rich bridge region separating the two active sites. Comparison with distantly related APRTases reveal similarities and differences of the active site.

AB - Adenine phosphoribosyltransferase (APRTase) is a widely distributed enzyme involved in the salvage of adenine to form an adenine nucleotide. We crystallized and determined the X-ray crystallographic structure of a purine/pyrimidine phosphoribosyltransferase-related protein from the thermophilic bacterium, Thermus thermophilus HB8. The crystal space group was C2 with unit cell dimensions of a = 167.42 Å, b = 61.41 Å, c = 102.39 Å, β = 94.0°. Initial phases were determined to 2.6 Å using the multiple wavelength anomalous dispersion method and selenomethionine substituted protein (Se-MAD), and refined using a 1.9 Å "native" data set. The asymmetric unit contains two pairs of identical dinners, each related by noncrystallographic two-fold symmetry. The fifth monomer forms a similar dinner across a crystallographic two-fold axis. These dimers appear to be the biological unit with both monomers contributing to an unusual highly charged arginine-rich bridge region separating the two active sites. Comparison with distantly related APRTases reveal similarities and differences of the active site.

KW - Adenosine phosphoribosyltransferase

KW - X-ray

UR - http://www.scopus.com/inward/record.url?scp=27544503453&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=27544503453&partnerID=8YFLogxK

U2 - 10.1002/prot.20624

DO - 10.1002/prot.20624

M3 - Article

VL - 61

SP - 658

EP - 665

JO - Proteins: Structure, Function and Bioinformatics

JF - Proteins: Structure, Function and Bioinformatics

SN - 0887-3585

IS - 3

ER -