2gbm
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(New page: 200px<br /> <applet load="2gbm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gbm, resolution 1.55Å" /> '''Crystal Structure o...)
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Revision as of 20:10, 12 November 2007
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Crystal Structure of the 35-36 8 Glycine Insertion Mutant of Ubiquitin
Overview
We previously concluded that, judging from NMR chemical shifts, the, effects of insertions into ubiquitin on its conformation appear to depend, primarily on the site of insertion rather than the sequence of the, insertion. To obtain a more complete and atomic-resolution understanding, of how these insertions modulate the conformation of ubiquitin, we have, solved the crystal structures of four insertional mutants of ubiquitin., Insertions between residues 9 and 10 of ubiquitin are minimally perturbing, to the remainder of the protein, while larger alterations occur when the, insertion is between residues 35 and 36. Further, the alterations in, response to insertions are very similar for each mutant at a given site., Two insertions, one at each site, were designed from structurally, homologous proteins. Interestingly, the secondary structure within these, five to seven amino acid residue insertions is conserved in the new, protein. Overall, the crystal structures support the previous conclusion, that the conformational effects of these insertions are determined largely, by the site of insertion and only secondarily by the sequence of the, insert.
About this Structure
2GBM is a Single protein structure of sequence from Homo sapiens with ARS as ligand. Full crystallographic information is available from OCA.
Reference
Structures of ubiquitin insertion mutants support site-specific reflex response to insertions hypothesis., Ferraro DM, Ferraro DJ, Ramaswamy S, Robertson AD, J Mol Biol. 2006 Jun 2;359(2):390-402. Epub 2006 Apr 5. PMID:16647719
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