This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The enzymes RebC and StaC share a common substrate and 67% homology, yet make different products along separate natural product biosynthetic pathways;RebC and StaC are involved in rebeccamycin and staurosporine biosynthesis, respectively. Their reactivities seem to be regulated by the enzymes'FAD binding affinities. Mutation of key residues in RebC has resulted in a """"""""StaC-like"""""""" enzyme in both activity and FAD binding, and we now seek to obtain a crystal structure that might explain these changes.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR015301-08
Application #
8169294
Study Section
Special Emphasis Panel (ZRG1-BCMB-K (40))
Project Start
2010-04-01
Project End
2011-03-31
Budget Start
2010-04-01
Budget End
2011-03-31
Support Year
8
Fiscal Year
2010
Total Cost
$4,083
Indirect Cost
Name
Cornell University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
872612445
City
Ithaca
State
NY
Country
United States
Zip Code
14850
Chen, Wenyang; Mandali, Sridhar; Hancock, Stephen P et al. (2018) Multiple serine transposase dimers assemble the transposon-end synaptic complex during IS607-family transposition. Elife 7:
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