Structural highlights
Function
NPII_ASPOR Metalloprotease that shows high activities on basic nuclear substrates such as histone and protamine.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A data set from the metalloproteinase deuterolysin was collected at atomic resolution (1.0 A) with synchrotron radiation. The high resolution allowed the structure to be solved with the new direct-methods program ACORN using the coordinates of the Zn atom as a starting point. The phases obtained from ACORN were of sufficient quality to allow automated building to be carried out in ARP/wARP. Minimal manual rebuilding of the model was required and the structure determination was completed using the maximum-likelihood refinement program REFMAC. The whole process, starting from the processed and merged data and ending with a refined model, required less than 6 h of computational time.
A quick solution: ab initio structure determination of a 19 kDa metalloproteinase using ACORN.,McAuley KE, Jia-Xing Y, Dodson EJ, Lehmbeck J, Ostergaard PR, Wilson KS Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1571-8. Epub 2001, Oct 25. PMID:11679721[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ McAuley KE, Jia-Xing Y, Dodson EJ, Lehmbeck J, Ostergaard PR, Wilson KS. A quick solution: ab initio structure determination of a 19 kDa metalloproteinase using ACORN. Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1571-8. Epub 2001, Oct 25. PMID:11679721
