An interfacial mechanism and a class of inhibitors inferred from two crystal structures of the Mycobacterium tuberculosis 30 kDa major secretory protein (Antigen 85B), a mycolyl transferase.

@article{Anderson2001AnIM,
  title={An interfacial mechanism and a class of inhibitors inferred from two crystal structures of the Mycobacterium tuberculosis 30 kDa major secretory protein (Antigen 85B), a mycolyl transferase.},
  author={Daniel H Anderson and Guenter Harth and Marcus A. Horwitz and David S Eisenberg},
  journal={Journal of molecular biology},
  year={2001},
  volume={307 2},
  pages={
          671-81
        }
}
The Mycobacterium tuberculosis 30 kDa major secretory protein (antigen 85B) is the most abundant protein exported by M. tuberculosis, as well as a potent immunoprotective antigen and a leading drug target. A mycolyl transferase of 285 residues, it is closely related to two other mycolyl transferases, each of molecular mass 32 kDa: antigen 85A and antigen 85C. All three catalyze transfer of the fatty acid mycolate from one trehalose monomycolate to another, resulting in trehalose dimycolate and… CONTINUE READING
Highly Cited
This paper has 98 citations. REVIEW CITATIONS

Citations

Publications citing this paper.
Showing 1-10 of 47 extracted citations

99 Citations

01020'01'04'08'12'16
Citations per Year
Semantic Scholar estimates that this publication has 99 citations based on the available data.

See our FAQ for additional information.

References

Publications referenced by this paper.
Showing 1-10 of 42 references

SHELXL: high-resolution refinement.

Methods in enzymology • 1997
View 5 Excerpts
Highly Influenced

Practical Protein Crystallography

D. McRee
1993
View 4 Excerpts
Highly Influenced