3.0-A RESOLUTION STUDY OF NUCLEOTIDE COMPLEXES WITH ASPARTATE CARBAMOYLTRANSFERASE

被引：24

作者：

HONZATKO, RB ^{[1
]}

MONACO, HL ^{[1
]}

LIPSCOMB, WN ^{[1
]}

机构：

[1] HARVARD UNIV,GIBBS CHEM LAB,CAMBRIDGE,MA 02138

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1979年 / 76卷 / 10期

关键词：

D O I：

10.1073/pnas.76.10.5105

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The binding sites of CTP, CDP, 5-BrCTP, and ATP to the allosteric site of aspartate carbamoyltransferase (carbamoylphosphate:L-aspartate carbamoyltransferase, EC 2.1.3.2) have been found in electron-density maps obtained at about 3 A resolution from x-ray diffraction studies of single crystals. The activator ATP binds in the anti conformation, whereas the inhibitor 5-BrCTP binds in the syn conformation. Both activator and inhibitor bind to the same local region of the enzyme. All of the cytidine nucleotides show important interactions of the base with the protein. The triphosphate conformations are similar, whereas the terminal phosphate of CDP occupies the site of the gamma-phosphate of CTP, thus implying a protein-nucleotide interaction at this site. These results are then related to biochemical studies.

引用

页码：5105 / 5109

页数：5

共 31 条

[21] NUCLEAR MAGNETIC RESONANCE STUDY OF METAL-ION BINDING TO ADENOSINE TRIPHOSPHATE .2. PROTON STUDIES [J].