ACM SIGGRAPH International Conference on

1
ACM SIGGRAPH International Conference on
Virtual Reality Continuum and Its Applications
in Industry Nanyang Technological University,
Singapore, June 16-18, 2004


Crystal Structure of Rv2002 Gene Product from
Mycobacterium Tuberculosis (1NNF) Seow Joo
Hong Nanyang University

Fig 1. Primary Structure
Fig 2. Secondary Structure
Fig 4. Ligands
Fig 3. Space filling

It is possible to perform whole scale gene
expression in E-coli where the expressed proteins
may not fold properly and may accumulate as
inclusion bodies. A conventional way to overcome
the solubility difficulty is site-directed
mutagenesis of one or a few amino acids which
will be slow and extensive effort required. A new
directed evolution strategy which the gene
encoding the protein is subjected to random
mutations and the soluble mutants are selected by
the coding GFP ( Green Fluorescent Protein).
Figures 1-4 illustrates the structure of the
proteins. The target protein is fused to
N-terminus of the GFP. The GFP folds properly and
emits green light only when the upstream target
mutant protein folds properly (Fig 5).
Fig 5. Target Mutant
Rv2002 a reduction enzyme in mycobacterium
tuberculosis was used as an example. Random
mutagenesis and selections rendered a dramatic
improvement in the molecules solubility when
expressed in E-coli.
STAM, J. 2001. A Simple Fluid Solver Based on the
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