Abstract |
Adenylosuccinate lyase (ASL) from Bacillus subtilis has been crystallized and structural analysis by X-ray diffraction is in progress. ASL is a 200-kDa homotetramer that catalyzes two distinct steps of de novo purine biosynthesis leading to the formation of AMP and IMP; both steps involve the beta-elimination of fumarate. A single point mutation in the human ASL gene has been linked to mental retardation with autistic features. In addition, ASL plays an important role in the bioprocessing of anti-HIV therapeutics. B subtilis ASL, which shares 30% sequence identity and 70% sequence similarity with human ASL, has been crystallized and data to 3.3 A have been collected at 100 K. The space group is P6(1)22 or P6(5)22 with a = b = 129.4 A; the length of the c-axis varies between 275 and 290 A, depending on the crystal. An analysis of solvent content indicates a dimer in the asymmetric unit, although a self-rotation function and an analysis of native Pattersons failed to identify unambiguously the location of any noncrystallographic symmetry axes. Structure determination by isomorphous replacement is in progress.
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Authors | M R Redinbo, S M Eide, R L Stone, J E Dixon, T O Yeates |
Journal | Protein science : a publication of the Protein Society
(Protein Sci)
Vol. 5
Issue 4
Pg. 786-8
(Apr 1996)
ISSN: 0961-8368 [Print] United States |
PMID | 8845770
(Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)
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Chemical References |
- Purines
- Adenylosuccinate Lyase
- purine
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Topics |
- Adenylosuccinate Lyase
(chemistry)
- Autistic Disorder
(enzymology)
- Bacillus subtilis
(enzymology)
- Crystallization
- Crystallography, X-Ray
- Humans
- Purines
(biosynthesis)
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