|
Originally published In Press as doi:10.1074/jbc.M401336200 on March 12, 2004
J. Biol. Chem., Vol. 279, Issue 22, 23447-23452, May 28, 2004
Crystal Structure of Yeast Allantoicase Reveals a Repeated Jelly Roll Motif*
Nicolas Leulliot ,
Sophie Quevillon-Cheruel ,
Isabelle Sorel ,
Marc Graille ,
Philippe Meyer ,
Dominique Liger ,
Karine Blondeau¶,
Joël Janin , and
Herman van Tilbeurgh ||
From the
Institut de Biochimie et de Biophysique Moléculaire et Cellulaire (CNRS-Unité Mixte de Recherche 8619), Université Paris-Sud, Bâtiment 430, 91405 Orsay, Laboratoire d'Enzymologie et Biochimie Structurales (CNRS-Unité Propre de Recherche 9063), Bâtiment 34, 1 Avenue de la Terrasse, 91198 Gif sur Yvette, and ¶Institut de Génétique et Microbiologie (CNRS-Unité Mixte de Recherche 8621), Université Paris-Sud, Bâtiment 360, 91405 Orsay, France
Allantoicase (EC 3.5.3.4) catalyzes the conversion of allantoate into ureidoglycolate and urea, one of the final steps in the degradation of purines to urea. The mechanism of most enzymes involved in this pathway, which has been known for a long time, is unknown. In this paper we describe the three-dimensional crystal structure of the yeast allantoicase determined at a resolution of 2.6 Å by single anomalous diffraction. This constitutes the first structure for an enzyme of this pathway. The structure reveals a repeated jelly roll -sheet motif, also present in proteins of unrelated biochemical function. Allantoicase has a hexameric arrangement in the crystal (dimer of trimers). Analysis of the protein sequence against the structural data reveals the presence of two totally conserved surface patches, one on each jelly roll motif. The hexameric packing concentrates these patches into conserved pockets that probably constitute the active site.
Received for publication, February 6, 2004
, and in revised form, March 4, 2004.
The atomic coordinates and structure factors (code 1SG3) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).
* This work was supported by grants from the Ministère de la Recherche et de la Technologie (Programme Génopoles) and the Association pour la Recherche contre le Cancer (to M. G.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
|| To whom correspondence should be addressed. Tel.: 33-1-69-82-34-91; Fax: 33-1-69-82-31-29; E-mail: herman{at}lebs.cnrs-gif.fr.

CiteULike Complore Connotea Del.icio.us Digg Reddit Technorati What's this?
This article has been cited by other articles:

|
 |

|
 |
 
S. Quevillon-Cheruel, N. Leulliot, C. A. Muniz, M. Vincent, J. Gallay, M. Argentini, D. Cornu, F. Boccard, B. Lemaitre, and H. van Tilbeurgh
Evf, a Virulence Factor Produced by the Drosophila Pathogen Erwinia carotovora, Is an S-Palmitoylated Protein with a New Fold That Binds to Lipid Vesicles
J. Biol. Chem.,
February 6, 2009;
284(6):
3552 - 3562.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
F. Robin, J. Delmas, C. Schweitzer, O. Tournilhac, O. Lesens, C. Chanal, and R. Bonnet
Evolution of TEM-Type Enzymes: Biochemical and Genetic Characterization of Two New Complex Mutant TEM Enzymes, TEM-151 and TEM-152, from a Single Patient
Antimicrob. Agents Chemother.,
April 1, 2007;
51(4):
1304 - 1309.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
F. Robin, J. Delmas, M. Archambaud, C. Schweitzer, C. Chanal, and R. Bonnet
CMT-Type {beta}-Lactamase TEM-125, an Emerging Problem for Extended-Spectrum {beta}-Lactamase Detection.
Antimicrob. Agents Chemother.,
July 1, 2006;
50(7):
2403 - 2408.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
J. Delmas, F. Robin, F. Carvalho, C. Mongaret, and R. Bonnet
Prediction of the Evolution of Ceftazidime Resistance in Extended-Spectrum {beta}-Lactamase CTX-M-9
Antimicrob. Agents Chemother.,
February 1, 2006;
50(2):
731 - 738.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
E. W. Odom and G. R. Vasta
Characterization of a Binary Tandem Domain F-type Lectin from Striped Bass (Morone saxatilis)
J. Biol. Chem.,
January 20, 2006;
281(3):
1698 - 1713.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
C. D. Todd, P. A. Tipton, D. G. Blevins, P. Piedras, M. Pineda, and J. C. Polacco
Update on ureide degradation in legumes
J. Exp. Bot.,
January 1, 2006;
57(1):
5 - 12.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
F. Robin, J. Delmas, C. Chanal, D. Sirot, J. Sirot, and R. Bonnet
TEM-109 (CMT-5), a Natural Complex Mutant of TEM-1 {beta}-Lactamase Combining the Amino Acid Substitutions of TEM-6 and TEM-33 (IRT-5)
Antimicrob. Agents Chemother.,
November 1, 2005;
49(11):
4443 - 4447.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
J. Delmas, F. Robin, F. Bittar, C. Chanal, and R. Bonnet
Unexpected Enzyme TEM-126: Role of Mutation Asp179Glu
Antimicrob. Agents Chemother.,
October 1, 2005;
49(10):
4280 - 4287.
[Abstract]
[Full Text]
[PDF]
|
 |
|
Copyright © 2004 by the American Society for Biochemistry and Molecular Biology.
|
Advertisement
Advertisement
|