Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture

Min Sung Kim, Joon Shin, Weon Tae Lee, Heung Soo Lee, Byung Ha Oh

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

RbsD is the only protein whose biochemical function is unknown among the six gene products of the rbs operon involved in the active transport of ribose. FucU, a paralogue of RbsD conserved from bacteria to human, is also the only protein whose function is unknown among the seven gene products of the L-fucose regulon. Here we report the crystal structures of Bacillus subtilis RbsD, which reveals a novel decameric toroidal assembly of the protein. Nuclear magnetic resonance and other studies on RbsD reveal that the intersubunit cleft of the protein binds specific forms of D-ribose, but it does not have an enzyme activity toward the sugar. Likewise, FucU binds L-fucose but lacks an enzyme activity toward this sugar. We conclude that RbsD and FucU are cytoplasmic sugar-binding proteins, a novel class of proteins whose functional role may lie in helping influx of the sugar substrates.

Original languageEnglish
Pages (from-to)28173-28180
Number of pages8
JournalJournal of Biological Chemistry
Volume278
Issue number30
DOIs
Publication statusPublished - 2003 Jul 25

Fingerprint

Sugars
Carrier Proteins
Crystal structure
Ribose
Fucose
Enzyme activity
Proteins
Genes
Regulon
Active Biological Transport
Bacilli
Enzymes
Operon
Bacillus subtilis
Bacteria
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
Substrates

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

@article{73bab122034f4572840b8077dd3dc8bd,
title = "Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture",
abstract = "RbsD is the only protein whose biochemical function is unknown among the six gene products of the rbs operon involved in the active transport of ribose. FucU, a paralogue of RbsD conserved from bacteria to human, is also the only protein whose function is unknown among the seven gene products of the L-fucose regulon. Here we report the crystal structures of Bacillus subtilis RbsD, which reveals a novel decameric toroidal assembly of the protein. Nuclear magnetic resonance and other studies on RbsD reveal that the intersubunit cleft of the protein binds specific forms of D-ribose, but it does not have an enzyme activity toward the sugar. Likewise, FucU binds L-fucose but lacks an enzyme activity toward this sugar. We conclude that RbsD and FucU are cytoplasmic sugar-binding proteins, a novel class of proteins whose functional role may lie in helping influx of the sugar substrates.",
author = "Kim, {Min Sung} and Joon Shin and Lee, {Weon Tae} and Lee, {Heung Soo} and Oh, {Byung Ha}",
year = "2003",
month = "7",
day = "25",
doi = "10.1074/jbc.M304523200",
language = "English",
volume = "278",
pages = "28173--28180",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "30",

}

Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture. / Kim, Min Sung; Shin, Joon; Lee, Weon Tae; Lee, Heung Soo; Oh, Byung Ha.

In: Journal of Biological Chemistry, Vol. 278, No. 30, 25.07.2003, p. 28173-28180.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture

AU - Kim, Min Sung

AU - Shin, Joon

AU - Lee, Weon Tae

AU - Lee, Heung Soo

AU - Oh, Byung Ha

PY - 2003/7/25

Y1 - 2003/7/25

N2 - RbsD is the only protein whose biochemical function is unknown among the six gene products of the rbs operon involved in the active transport of ribose. FucU, a paralogue of RbsD conserved from bacteria to human, is also the only protein whose function is unknown among the seven gene products of the L-fucose regulon. Here we report the crystal structures of Bacillus subtilis RbsD, which reveals a novel decameric toroidal assembly of the protein. Nuclear magnetic resonance and other studies on RbsD reveal that the intersubunit cleft of the protein binds specific forms of D-ribose, but it does not have an enzyme activity toward the sugar. Likewise, FucU binds L-fucose but lacks an enzyme activity toward this sugar. We conclude that RbsD and FucU are cytoplasmic sugar-binding proteins, a novel class of proteins whose functional role may lie in helping influx of the sugar substrates.

AB - RbsD is the only protein whose biochemical function is unknown among the six gene products of the rbs operon involved in the active transport of ribose. FucU, a paralogue of RbsD conserved from bacteria to human, is also the only protein whose function is unknown among the seven gene products of the L-fucose regulon. Here we report the crystal structures of Bacillus subtilis RbsD, which reveals a novel decameric toroidal assembly of the protein. Nuclear magnetic resonance and other studies on RbsD reveal that the intersubunit cleft of the protein binds specific forms of D-ribose, but it does not have an enzyme activity toward the sugar. Likewise, FucU binds L-fucose but lacks an enzyme activity toward this sugar. We conclude that RbsD and FucU are cytoplasmic sugar-binding proteins, a novel class of proteins whose functional role may lie in helping influx of the sugar substrates.

UR - http://www.scopus.com/inward/record.url?scp=0041344457&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0041344457&partnerID=8YFLogxK

U2 - 10.1074/jbc.M304523200

DO - 10.1074/jbc.M304523200

M3 - Article

C2 - 12738765

AN - SCOPUS:0041344457

VL - 278

SP - 28173

EP - 28180

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 30

ER -