Abstract
We describe the successful design of a tetrahedral His3Cys Zn(II)-binding site in a small protein of known structure: the B1 domain of Streptococcal protein G. The B1 variants containing the novel metal-binding site were characterized using a combination of optical absorption, circular dichroism and NMR spectroscopies. The results indicate that the designed proteins bind Zn(II) with high affinity and tetrahedral coordination geometry, and that the overall secondary and tertiary structure of the B1 domain is maintained.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 368-373 |
| Number of pages | 6 |
| Journal | Nature Structural Biology |
| Volume | 2 |
| Issue number | 5 |
| State | Published - May 1995 |
Fingerprint
ASJC Scopus subject areas
- Biochemistry
- Genetics
- Structural Biology
Cite this
Novel metal-binding proteins by design. / Klemba, Michael; Gardner, Kevin H.; Marino, Stephen; Clarke, Neil D.; Regan, Lynne.
In: Nature Structural Biology, Vol. 2, No. 5, 05.1995, p. 368-373.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Novel metal-binding proteins by design
AU - Klemba, Michael
AU - Gardner, Kevin H.
AU - Marino, Stephen
AU - Clarke, Neil D.
AU - Regan, Lynne
PY - 1995/5
Y1 - 1995/5
N2 - We describe the successful design of a tetrahedral His3Cys Zn(II)-binding site in a small protein of known structure: the B1 domain of Streptococcal protein G. The B1 variants containing the novel metal-binding site were characterized using a combination of optical absorption, circular dichroism and NMR spectroscopies. The results indicate that the designed proteins bind Zn(II) with high affinity and tetrahedral coordination geometry, and that the overall secondary and tertiary structure of the B1 domain is maintained.
AB - We describe the successful design of a tetrahedral His3Cys Zn(II)-binding site in a small protein of known structure: the B1 domain of Streptococcal protein G. The B1 variants containing the novel metal-binding site were characterized using a combination of optical absorption, circular dichroism and NMR spectroscopies. The results indicate that the designed proteins bind Zn(II) with high affinity and tetrahedral coordination geometry, and that the overall secondary and tertiary structure of the B1 domain is maintained.
UR - http://www.scopus.com/inward/record.url?scp=0029017933&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0029017933&partnerID=8YFLogxK
M3 - Article
C2 - 7664093
AN - SCOPUS:0029017933
VL - 2
SP - 368
EP - 373
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
SN - 1545-9993
IS - 5
ER -