Structure of SAICAR synthase from Thermotoga maritima at 2.2 Å reveals an unusual covalent dimer
Abstract
The crystal structure of phophoribosylaminoimidazole-succinocarboxamide or SAICAR synthase from T. maritima at 2.2 Å revealed an unusual covalent dimer. As a part of a structural genomics program, the 2.2 Å resolution crystal structure of the PurC gene product from Thermotoga maritima has been solved. This 26.2 kDa protein belongs to the phophoribosylaminoimidazole-succinocarboxamide or SAICAR synthase family of enzymes, the members of which are involved in de novo purine biosynthesis. SAICAR synthase can be divided into three subdomains: two α+β regions exhibiting structural homology with ATP-binding proteins and a carboxy-terminal subdomain of two α-helices. The asymmetric unit contains two copies of the protein which are covalently linked by a disulfide bond between Cys126(A) and Cys126(B). This 230-amino-acid protein exhibits high structural homology with SAICAR synthase from baker’s yeast. The protein structure is described and compared with that of the ATP–SAICAR synthase complex from yeast.
- Authors:
-
- Biosciences Division, Midwest Center for Structural Genomics, Structural Biology Center, Argonne National Laboratory, Argonne, IL 60439 (United States)
- Ontario Centre for Structural Proteomics, University of Toronto, University Health Network, Toronto, Ontario M5G 1L7 (Canada)
- (Canada)
- Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario M5G 1L6 (Canada)
- Department of Crystallography, Birkbeck College, Malet Street, London WC1E 7HX (United Kingdom)
- Publication Date:
- OSTI Identifier:
- 22356350
- Resource Type:
- Journal Article
- Resource Relation:
- Journal Name: Acta Crystallographica. Section F; Journal Volume: 62; Journal Issue: Pt 4; Other Information: PMCID: PMC2222583; PMID: 16582479; PUBLISHER-ID: tb5003; OAI: oai:pubmedcentral.nih.gov:2222583; Copyright (c) International Union of Crystallography 2006; This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html.; Country of input: International Atomic Energy Agency (IAEA)
- Country of Publication:
- United Kingdom
- Language:
- English
- Subject:
- 75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTAL STRUCTURE; DIMERS; PROTEIN STRUCTURE; RESOLUTION
Citation Formats
Zhang, Rongguang, Skarina, Tatiana, Evdokimova, Elena, Edwards, Aled, Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario M5G 1L6, Savchenko, Alexei, Laskowski, Roman, Cuff, Marianne E., and Joachimiak, Andrzej, E-mail: andrzejj@anl.gov. Structure of SAICAR synthase from Thermotoga maritima at 2.2 Å reveals an unusual covalent dimer. United Kingdom: N. p., 2006.
Web. doi:10.1107/S1744309106009651.
Zhang, Rongguang, Skarina, Tatiana, Evdokimova, Elena, Edwards, Aled, Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario M5G 1L6, Savchenko, Alexei, Laskowski, Roman, Cuff, Marianne E., & Joachimiak, Andrzej, E-mail: andrzejj@anl.gov. Structure of SAICAR synthase from Thermotoga maritima at 2.2 Å reveals an unusual covalent dimer. United Kingdom. doi:10.1107/S1744309106009651.
Zhang, Rongguang, Skarina, Tatiana, Evdokimova, Elena, Edwards, Aled, Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario M5G 1L6, Savchenko, Alexei, Laskowski, Roman, Cuff, Marianne E., and Joachimiak, Andrzej, E-mail: andrzejj@anl.gov. Sat .
"Structure of SAICAR synthase from Thermotoga maritima at 2.2 Å reveals an unusual covalent dimer". United Kingdom.
doi:10.1107/S1744309106009651.
@article{osti_22356350,
title = {Structure of SAICAR synthase from Thermotoga maritima at 2.2 Å reveals an unusual covalent dimer},
author = {Zhang, Rongguang and Skarina, Tatiana and Evdokimova, Elena and Edwards, Aled and Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario M5G 1L6 and Savchenko, Alexei and Laskowski, Roman and Cuff, Marianne E. and Joachimiak, Andrzej, E-mail: andrzejj@anl.gov},
abstractNote = {The crystal structure of phophoribosylaminoimidazole-succinocarboxamide or SAICAR synthase from T. maritima at 2.2 Å revealed an unusual covalent dimer. As a part of a structural genomics program, the 2.2 Å resolution crystal structure of the PurC gene product from Thermotoga maritima has been solved. This 26.2 kDa protein belongs to the phophoribosylaminoimidazole-succinocarboxamide or SAICAR synthase family of enzymes, the members of which are involved in de novo purine biosynthesis. SAICAR synthase can be divided into three subdomains: two α+β regions exhibiting structural homology with ATP-binding proteins and a carboxy-terminal subdomain of two α-helices. The asymmetric unit contains two copies of the protein which are covalently linked by a disulfide bond between Cys126(A) and Cys126(B). This 230-amino-acid protein exhibits high structural homology with SAICAR synthase from baker’s yeast. The protein structure is described and compared with that of the ATP–SAICAR synthase complex from yeast.},
doi = {10.1107/S1744309106009651},
journal = {Acta Crystallographica. Section F},
number = Pt 4,
volume = 62,
place = {United Kingdom},
year = {Sat Apr 01 00:00:00 EST 2006},
month = {Sat Apr 01 00:00:00 EST 2006}
}
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