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Crystallization and preliminary structural analysis of Bacillus subtilis adenylosuccinate lyase, an enzyme implicated in infantile autism.

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.
AuthorsM R Redinbo, S M Eide, R L Stone, J E Dixon, T O Yeates
JournalProtein science : a publication of the Protein Society (Protein Sci) Vol. 5 Issue 4 Pg. 786-8 (Apr 1996) ISSN: 0961-8368 [Print] United States
PMID8845770 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)
Chemical References
  • Purines
  • Adenylosuccinate Lyase
  • purine
Topics
  • Adenylosuccinate Lyase (chemistry)
  • Autistic Disorder (enzymology)
  • Bacillus subtilis (enzymology)
  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Purines (biosynthesis)

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