4.0 Article

Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of leucine aminopeptidase (LAP) from the pepA gene of Xanthomonas oryzae pv. oryzae

Publisher

INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309109031467

Keywords

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Funding

  1. Rural Development Administration, Republic of Korea [20070501034003]
  2. Ministry of Environment [173-091-006]
  3. Korea Science and Engineering Foundation (KOSEF) [R01-2008-000-20315-0]
  4. Korea Environmental Industry & Technology Institute (KEITI) [0520091700300060] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
  5. Ministry of Education, Science & Technology (MoST), Republic of Korea [R33-2008-000-10071-0] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
  6. National Research Foundation of Korea [2008-56529, R01-2008-000-20315-0] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
  7. Rural Development Administration (RDA), Republic of Korea [PJ00701220091136300, 20070501034003] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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Xanthomonas oryzae pv. oryzae (Xoo) causes the serious disease bacterial blight in rice. The pepA (Xoo0834) gene from Xoo is one of around 100 genes that have been selected for the design of antibacterial drugs. The pepA gene encodes leucine aminopeptidase (LAP), an exopeptidase that catalyzes the hydrolysis of leucine residues from the N-terminus of a protein or peptide. This enzyme was expressed in Escherichia coli, purified and crystallized, and preliminary X-ray structural studies have been carried out. The LAP crystal diffracted to 2.6 angstrom resolution and belonged to the cubic space group P2(1)3. The unit-cell volume of the crystal was compatible with the presence of two monomers in the asymmetric unit.

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