1KUT

Structural Genomics, Protein TM1243, (SAICAR synthetase)

Summary for 1KUT

• Entry DOI: 10.2210/pdb1kut/pdb
• Descriptor: Phosphoribosylaminoimidazole-succinocarboxamide synthase (2 entities in total)
• Functional Keywords: structural genomics, saicar synthetase, psi, protein structure initiative, midwest center for structural genomics, mcsg, ligase
• Biological source: Thermotoga maritima
• Total number of polymer chains: 2
• Total formula weight: 53016.13

Authors

Zhang, R.,Skarina, T.,Beasley, S.,Edwards, A.,Joachimiak, A.,Savchenko, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2002-01-22, release date: 2002-08-14, Last modification date: 2024-11-20)

Primary citation

Zhang, R.,Skarina, T.,Evdokimova, E.,Edwards, A.,Savchenko, A.,Laskowski, R.,Cuff, M.E.,Joachimiak, A.
Structure of SAICAR synthase from Thermotoga maritima at 2.2 angstroms reveals an unusual covalent dimer.
Acta Crystallogr.,Sect.F, 62:335-339, 2006

PubMed Abstract: As a part of a structural genomics program, the 2.2 angstroms 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 alpha+beta regions exhibiting structural homology with ATP-binding proteins and a carboxy-terminal subdomain of two alpha-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.

PubMed: 16582479
DOI: 10.1107/S1744309106009651

Experimental method

X-RAY DIFFRACTION (2.2 Å)