Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Open-closed conformational change revealed by the crystal structures of 3-keto-L-gulonate 6-phosphate decarboxylase from Streptococcus mutans

Li, Gui-Lan ; Liu, Xiang ; Nan, Jie LU orcid ; Brostromer, Erik ; Li, Lan-Fen and Su, Xiao-Dong LU (2009) In Biochemical and Biophysical Research Communications 381(3). p.33-429
Abstract

The 3-keto-L-gulonate 6-phosphate decarboxylase (KGPDC) catalyses the decarboxylation of 3-keto-L-gulonate 6-phosphate to L-xylulose in the presence of magnesium ions. The enzyme is involved in L-ascorbate metabolism and plays an essential role in the pathway of glucuronate interconversion. Crystal structures of Streptococcus mutans KGPDC were determined in the absence and presence of the product analog D-ribulose 5-phosphate. We have observed an 8 A alphaB-helix movement and other structural rearrangements around the active site between the apo-structures and product analog bound structure. These drastic conformational changes upon ligand binding are the first observation of this kind for the KGPDC family. The flexibilities of both the... (More)

The 3-keto-L-gulonate 6-phosphate decarboxylase (KGPDC) catalyses the decarboxylation of 3-keto-L-gulonate 6-phosphate to L-xylulose in the presence of magnesium ions. The enzyme is involved in L-ascorbate metabolism and plays an essential role in the pathway of glucuronate interconversion. Crystal structures of Streptococcus mutans KGPDC were determined in the absence and presence of the product analog D-ribulose 5-phosphate. We have observed an 8 A alphaB-helix movement and other structural rearrangements around the active site between the apo-structures and product analog bound structure. These drastic conformational changes upon ligand binding are the first observation of this kind for the KGPDC family. The flexibilities of both the alpha-helix lid and the side chains of Arg144 and Arg197 are associated with substrate binding and product releasing. The open-closed conformational changes of the active site, through the movements of the alpha-helix lid and the arginine residues are important for substrate binding and catalysis.

(Less)
Please use this url to cite or link to this publication:
author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
keywords
Amino Acid Sequence, Carboxy-Lyases, Catalytic Domain, Crystallography, X-Ray, Ligands, Molecular Sequence Data, Protein Structure, Secondary, Ribosemonophosphates, Streptococcus mutans
in
Biochemical and Biophysical Research Communications
volume
381
issue
3
pages
5 pages
publisher
Elsevier
external identifiers
  • scopus:62049084899
  • pmid:19222992
ISSN
1090-2104
DOI
10.1016/j.bbrc.2009.02.049
language
English
LU publication?
yes
id
9189afed-ff83-4e55-b318-521bf2d6712d
date added to LUP
2016-09-07 22:53:31
date last changed
2025-01-12 11:01:41
@article{9189afed-ff83-4e55-b318-521bf2d6712d,
  abstract     = {{<p>The 3-keto-L-gulonate 6-phosphate decarboxylase (KGPDC) catalyses the decarboxylation of 3-keto-L-gulonate 6-phosphate to L-xylulose in the presence of magnesium ions. The enzyme is involved in L-ascorbate metabolism and plays an essential role in the pathway of glucuronate interconversion. Crystal structures of Streptococcus mutans KGPDC were determined in the absence and presence of the product analog D-ribulose 5-phosphate. We have observed an 8 A alphaB-helix movement and other structural rearrangements around the active site between the apo-structures and product analog bound structure. These drastic conformational changes upon ligand binding are the first observation of this kind for the KGPDC family. The flexibilities of both the alpha-helix lid and the side chains of Arg144 and Arg197 are associated with substrate binding and product releasing. The open-closed conformational changes of the active site, through the movements of the alpha-helix lid and the arginine residues are important for substrate binding and catalysis.</p>}},
  author       = {{Li, Gui-Lan and Liu, Xiang and Nan, Jie and Brostromer, Erik and Li, Lan-Fen and Su, Xiao-Dong}},
  issn         = {{1090-2104}},
  keywords     = {{Amino Acid Sequence; Carboxy-Lyases; Catalytic Domain; Crystallography, X-Ray; Ligands; Molecular Sequence Data; Protein Structure, Secondary; Ribosemonophosphates; Streptococcus mutans}},
  language     = {{eng}},
  month        = {{04}},
  number       = {{3}},
  pages        = {{33--429}},
  publisher    = {{Elsevier}},
  series       = {{Biochemical and Biophysical Research Communications}},
  title        = {{Open-closed conformational change revealed by the crystal structures of 3-keto-L-gulonate 6-phosphate decarboxylase from Streptococcus mutans}},
  url          = {{http://dx.doi.org/10.1016/j.bbrc.2009.02.049}},
  doi          = {{10.1016/j.bbrc.2009.02.049}},
  volume       = {{381}},
  year         = {{2009}},
}