التفاصيل البيبلوغرافية
| العنوان: |
Crystallization and preliminary X-ray crystallographic analysis of malonyl-CoA decarboxylase from Rhizobium leguminosarum bv. trifolii |
| المؤلفون: |
Jung, JS, Baek, DJ, Lee, GY, Kim, YS, Oh, BH Oh, Byung-Ha |
| بيانات النشر: |
BLACKWELL PUBLISHING |
| سنة النشر: |
2003 |
| المجموعة: |
Korea Advanced Institute of Science and Technology: KOASAS - KAIST Open Access Self-Archiving System |
| الوصف: |
Malonyl-CoA decarboxylase (MCD), which catalyzes the conversion of malonyl-CoA to acetyl-CoA, is an evolutionarily distinct and highly conserved enzyme. MCD does not share sequence homology with other known decarboxylases, while the enzymes from different species exhibit at least >30% sequence identity to each other. In order to provide a canonical structure of the enzyme for detailed study of its structure-function relationship, the MCD of Rhizobium leguminosarum bv. trifolii was overexpressed and crystallized. The crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 133.45, b = 127.10, c = 66.37 Angstrom. The asymmetric unit is likely to contain two molecules of MCD (molecular weight of 51 418 Da), with a crystal volume per protein weight (V-M) of 2.69 Angstrom(3) Da(-1) and a solvent content of about 54.3% by volume. A native data set to 3.0 Angstrom resolution was obtained using a rotating-anode X-ray generator. ; 생명과학과 |
| نوع الوثيقة: |
article in journal/newspaper |
| اللغة: |
English |
| الإتاحة: |
http://hdl.handle.net/10203/85696Test |
| رقم الانضمام: |
edsbas.7DD4386A |
| قاعدة البيانات: |
BASE |
