Open-closed conformational change revealed by the crystal structures of 3-keto-L-gulonate 6-phosphate decarboxylase from Streptococcus mutans
(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)
- author
- Li, Gui-Lan ; Liu, Xiang ; Nan, Jie LU ; Brostromer, Erik ; Li, Lan-Fen and Su, Xiao-Dong LU
- organization
- publishing date
- 2009-04-10
- 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
- 2024-01-04 12:05:57
@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}},
}