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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