Crystallographic structure of an active, sequence-engineered ribonuclease.
نویسندگان
چکیده
منابع مشابه
Crystallographic structure of an active, sequence-engineered ribonuclease.
X-ray diffraction methods were used to test a synthetic-modeling approach to the sequence engineering of bovine pancreatic ribonuclease. A model of RNase S-peptide (residues 1-20), having a simplified amino acid sequence but retaining elements deduced to be essential for conformation and function, was previously synthesized and found to form a catalytically active and stable complex with native...
متن کاملAn X-ray and Crystallographic Study of Ribonuclease
A new crystalline protein of low molecular weight, ribonuclease, has been isolated and described by Kunitz (1, 2). A preliminary study of this protein has now been made with x-rays and with the polarizing microscope. The material studied was crystaUized from an ethanol-water solution. The crystals were dried in air without appreciable deterioration and the measurements here described were made ...
متن کاملCrystallographic analyses of an active HIV-1 ribonuclease H domain show structural features that distinguish it from the inactive form.
. An active recombinant preparation of the carboxy-terminal ribonuclease H (RNase H) domain of HIV-I reverse transcriptase has produced crystals of several different forms, including a trigonal prism form (P3(1); a = b = 52.03, c = 113.9 A with two molecules per asymmetric unit) and a hexagonal tablet form (P6(2)22 or P6(4)22; a = b = 93.5, c = 74.1 A with one molecule per asymmetric unit). The...
متن کاملActive Site of Ribonuclease A
Ribonuclease A (RNase A; EC 3.1.27.5) was perhaps the most studied enzyme of the 20th century and is the best characterized ribonuclease. The “A” in its name refers not to its substrate specificity, but to the predominant form of the enzyme produced by the bovine pancreas. RNase A is unmodified, whereas RNase B, RNase C, and RNase D are mixtures of glycoforms. Because of its availability in lar...
متن کاملAn active precursor in assembly of yeast nuclear ribonuclease P.
The RNA-protein subunit assembly of nuclear RNase P was investigated by specific isolation and characterization of the precursor and mature forms of RNase P using an RNA affinity ligand. Pre-RNase P was as active in pre-tRNA cleavage as mature RNase P, although it contained only seven of the nine proteins found in mature RNase P. Pop3p and Rpr2p were not required for maturation of the RPR1 RNA ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1985
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.82.19.6423