|Acta Crystallographica Section F: Structural Biology and Crystallization Communications (2006) 62(Pt 4):335-9|
|Midwest Center for Structural Genomics|
(click to unfold)
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.
|metabolism chemistry enzymology isolation & purification |
|Amino Acid Sequence Conserved Sequence Molecular Sequence Data Protein Structure, Secondary Sequence Alignment Cloning, Molecular Crystallization Sequence Homology, Amino Acid Recombinant Proteins Dimerization Saccharomyces cerevisiae Thermotoga maritima Peptide Synthases |
|12 (Last update: 08/11/2018 12:03:20pm)|