Structure of the Thermus thermophilus putative periplasmic glutamate/glutamine-binding protein

Hitomi Takahashi, Eiji Inagaki, Chizu Kuroishi, Tahir H Tahirov

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

As part of a structural genomics project, the crystal structure of a 314-amino-acid protein encoded by Thermus thermophilus HB8 gene TT1099 was solved to 1.75 Å using the multiple-wavelength anomalous dispersion (MAD) method and a selenomethionine-incorporated protein. The native protein structure was solved to 1.5 Å using the molecular-replacement method. Both structures revealed a bound ligand, L-glutamate or L-glutamine, and a fold related to the periplasmic substrate-binding proteins (PSBP). Further comparative structural analysis with other PSBP-fold proteins revealed the conservation of the predicted membrane permease binding surface area and indicated that the T. thermophilus HB8 molecule is most likely to be an L-glutamate and/or an L-glutamine-binding protein related to the cluster 3 periplasmic receptors. However, the geometry of ligand binding is unique to the T. thermophilus HB8 molecule.

Original languageEnglish (US)
Pages (from-to)1846-1854
Number of pages9
JournalActa Crystallographica Section D: Biological Crystallography
Volume60
Issue number10
DOIs
StatePublished - Oct 1 2004

Fingerprint

Thermus thermophilus
glutamine
glutamates
Glutamic Acid
Periplasmic Binding Proteins
proteins
Glutamine
Carrier Proteins
Proteins
Selenomethionine
Ligands
Molecules
Membrane Transport Proteins
Substrates
Genomics
Structural analysis
Conservation
Genes
Crystal structure
ligands

ASJC Scopus subject areas

  • Structural Biology
  • Medicine(all)

Cite this

Structure of the Thermus thermophilus putative periplasmic glutamate/glutamine-binding protein. / Takahashi, Hitomi; Inagaki, Eiji; Kuroishi, Chizu; Tahirov, Tahir H.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 60, No. 10, 01.10.2004, p. 1846-1854.

Research output: Contribution to journalArticle

@article{cf5d4629a36347368d86bf68a4bf0af9,
title = "Structure of the Thermus thermophilus putative periplasmic glutamate/glutamine-binding protein",
abstract = "As part of a structural genomics project, the crystal structure of a 314-amino-acid protein encoded by Thermus thermophilus HB8 gene TT1099 was solved to 1.75 {\AA} using the multiple-wavelength anomalous dispersion (MAD) method and a selenomethionine-incorporated protein. The native protein structure was solved to 1.5 {\AA} using the molecular-replacement method. Both structures revealed a bound ligand, L-glutamate or L-glutamine, and a fold related to the periplasmic substrate-binding proteins (PSBP). Further comparative structural analysis with other PSBP-fold proteins revealed the conservation of the predicted membrane permease binding surface area and indicated that the T. thermophilus HB8 molecule is most likely to be an L-glutamate and/or an L-glutamine-binding protein related to the cluster 3 periplasmic receptors. However, the geometry of ligand binding is unique to the T. thermophilus HB8 molecule.",
author = "Hitomi Takahashi and Eiji Inagaki and Chizu Kuroishi and Tahirov, {Tahir H}",
year = "2004",
month = "10",
day = "1",
doi = "10.1107/S0907444904019420",
language = "English (US)",
volume = "60",
pages = "1846--1854",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "0907-4449",
publisher = "John Wiley and Sons Inc.",
number = "10",

}

TY - JOUR

T1 - Structure of the Thermus thermophilus putative periplasmic glutamate/glutamine-binding protein

AU - Takahashi, Hitomi

AU - Inagaki, Eiji

AU - Kuroishi, Chizu

AU - Tahirov, Tahir H

PY - 2004/10/1

Y1 - 2004/10/1

N2 - As part of a structural genomics project, the crystal structure of a 314-amino-acid protein encoded by Thermus thermophilus HB8 gene TT1099 was solved to 1.75 Å using the multiple-wavelength anomalous dispersion (MAD) method and a selenomethionine-incorporated protein. The native protein structure was solved to 1.5 Å using the molecular-replacement method. Both structures revealed a bound ligand, L-glutamate or L-glutamine, and a fold related to the periplasmic substrate-binding proteins (PSBP). Further comparative structural analysis with other PSBP-fold proteins revealed the conservation of the predicted membrane permease binding surface area and indicated that the T. thermophilus HB8 molecule is most likely to be an L-glutamate and/or an L-glutamine-binding protein related to the cluster 3 periplasmic receptors. However, the geometry of ligand binding is unique to the T. thermophilus HB8 molecule.

AB - As part of a structural genomics project, the crystal structure of a 314-amino-acid protein encoded by Thermus thermophilus HB8 gene TT1099 was solved to 1.75 Å using the multiple-wavelength anomalous dispersion (MAD) method and a selenomethionine-incorporated protein. The native protein structure was solved to 1.5 Å using the molecular-replacement method. Both structures revealed a bound ligand, L-glutamate or L-glutamine, and a fold related to the periplasmic substrate-binding proteins (PSBP). Further comparative structural analysis with other PSBP-fold proteins revealed the conservation of the predicted membrane permease binding surface area and indicated that the T. thermophilus HB8 molecule is most likely to be an L-glutamate and/or an L-glutamine-binding protein related to the cluster 3 periplasmic receptors. However, the geometry of ligand binding is unique to the T. thermophilus HB8 molecule.

UR - http://www.scopus.com/inward/record.url?scp=13844290685&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=13844290685&partnerID=8YFLogxK

U2 - 10.1107/S0907444904019420

DO - 10.1107/S0907444904019420

M3 - Article

VL - 60

SP - 1846

EP - 1854

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 0907-4449

IS - 10

ER -