Publication Date:
2006-07-01
Description:
The formation of glutaminyl transfer RNA (Gln-tRNA(Gln)) differs among the three domains of life. Most bacteria employ an indirect pathway to produce Gln-tRNA(Gln) by a heterotrimeric glutamine amidotransferase CAB (GatCAB) that acts on the misacylated Glu-tRNA(Gln). Here, we describe a series of crystal structures of intact GatCAB from Staphylococcus aureus in the apo form and in the complexes with glutamine, asparagine, Mn2+, and adenosine triphosphate analog. Two identified catalytic centers for the glutaminase and transamidase reactions are markedly distant but connected by a hydrophilic ammonia channel 30 A in length. Further, we show that the first U-A base pair in the acceptor stem and the D loop of tRNA(Gln) serve as identity elements essential for discrimination by GatCAB and propose a complete model for the overall concerted reactions to synthesize Gln-tRNA(Gln).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakamura, Akiyoshi -- Yao, Min -- Chimnaronk, Sarin -- Sakai, Naoki -- Tanaka, Isao -- New York, N.Y. -- Science. 2006 Jun 30;312(5782):1954-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Faculty of Advanced Life Sciences, Hokkaido University, Sapporo 060-0810, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16809541" target="_blank"〉PubMed〈/a〉
Keywords:
Adenosine Diphosphate/metabolism
;
Amino Acid Sequence
;
Aminoacyltransferases/metabolism
;
Ammonia/*metabolism
;
Apoenzymes/chemistry/metabolism
;
Asparagine/metabolism
;
Base Pairing
;
Catalytic Domain
;
Crystallography, X-Ray
;
Glutaminase/metabolism
;
Glutamine/*chemistry/metabolism
;
Hydrogen Bonding
;
Hydrophobic and Hydrophilic Interactions
;
Magnesium/metabolism
;
Manganese/metabolism
;
Models, Molecular
;
Molecular Sequence Data
;
Mutation
;
Nucleic Acid Conformation
;
Protein Structure, Quaternary
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
Protein Subunits
;
RNA, Bacterial/chemistry/metabolism
;
RNA, Transfer, Amino Acyl/chemistry/*metabolism
;
RNA, Transfer, Gln/*chemistry/metabolism
;
Staphylococcus aureus/*enzymology/genetics/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
