Publication Date:
1987-09-25
Description:
Previous experimental results along with the structural modeling presented indicate that a nucleotide fold starts in the amino-terminal part of Escherichia coli isoleucyl-transfer RNA synthetase, a single chain polypeptide of 939 amino acids. Internal deletions were created in the region of the nucleotide fold. A set of deletions that collectively span 145 contiguous amino acids yielded active enzymes. Further extensions of the deletions yielded inactive or unstable proteins. The three-dimensional structure of an evidently homologous protein suggests that the active deletions lack portions of a segment that connects two parts of the nucleotide fold. Therefore, the results imply that removal of major sections of the polypeptide that connects these two parts of the fold does not result in major perturbation of the nucleotide binding site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Starzyk, R M -- Webster, T A -- Schimmel, P -- GM23562/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Sep 25;237(4822):1614-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3306924" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
*Amino Acyl-tRNA Synthetases
;
Bacterial Proteins
;
Binding Sites
;
Escherichia coli/enzymology
;
Hydrogen Bonding
;
*Isoleucine-tRNA Ligase
;
*Methionine-tRNA Ligase
;
Protein Conformation
;
RNA, Transfer/*metabolism
;
Structure-Activity Relationship
;
Transfer RNA Aminoacylation
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
Permalink
