PMID- 10430027
OWN - NLM
STAT- MEDLINE
DCOM- 19990831
LR  - 20131121
IS  - 1431-6730 (Print)
IS  - 1431-6730 (Linking)
VI  - 380
IP  - 6
DP  - 1999 Jun
TI  - Histidyl-tRNA synthetase.
PG  - 623-46
AB  - Histidyl-tRNA synthetase (HisRS) is responsible for the synthesis of
      histidyl-transfer RNA, which is essential for the incorporation of histidine into
      proteins. This amino acid has uniquely moderate basic properties and is an
      important group in many catalytic functions of enzymes. A compilation of
      currently known primary structures of HisRS shows that the subunits of these
      homo-dimeric enzymes consist of 420-550 amino acid residues. This represents a
      relatively short chain length among aminoacyl-tRNA synthetases (aaRS), whose
      peptide chain sizes range from about 300 to 1100 amino acid residues. The crystal
      structures of HisRS from two organisms and their complexes with histidine,
      histidyl-adenylate and histidinol with ATP have been solved. HisRS from
      Escherichia coli and Thermus thermophilus are very similar dimeric enzymes
      consisting of three domains: the N-terminal catalytic domain containing the
      six-stranded antiparallel beta-sheet and the three motifs characteristic of class
      II aaRS, a HisRS-specific helical domain inserted between motifs 2 and 3 that may
      contact the acceptor stem of the tRNA, and a C-terminal alpha/beta domain that
      may be involved in the recognition of the anticodon stem and loop of tRNA(His).
      The aminoacylation reaction follows the standard two-step mechanism. HisRS also
      belongs to the group of aaRS that can rapidly synthesize diadenosine
      tetraphosphate, a compound that is suspected to be involved in several regulatory
      mechanisms of cell metabolism. Many analogs of histidine have been tested for
      their properties as substrates or inhibitors of HisRS, leading to the elucidation
      of structure-activity relationships concerning configuration, importance of the
      carboxy and amino group, and the nature of the side chain. HisRS has been found
      to act as a particularly important antigen in autoimmune diseases such as
      rheumatic arthritis or myositis. Successful attempts have been made to identify
      epitopes responsible for the complexation with such auto-antibodies.
FAU - Freist, W
AU  - Freist W
AD  - Max-Planck-Institut fur experimentelle Medizin, Abteilung Molekulare Biologie
      Neuronaler Signale, Gottingen, Germany.
FAU - Verhey, J F
AU  - Verhey JF
FAU - Ruhlmann, A
AU  - Ruhlmann A
FAU - Gauss, D H
AU  - Gauss DH
FAU - Arnez, J G
AU  - Arnez JG
LA  - eng
PT  - Journal Article
PT  - Review
PL  - Germany
TA  - Biol Chem
JT  - Biological chemistry
JID - 9700112
RN  - 0 (RNA, Transfer, His)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - EC 6.1.1.21 (Histidine-tRNA Ligase)
SB  - IM
MH  - Adenosine Triphosphate/metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - Autoimmune Diseases/enzymology
MH  - Histidine-tRNA Ligase/chemistry/genetics/*metabolism
MH  - Humans
MH  - Molecular Sequence Data
MH  - Nucleic Acid Conformation
MH  - RNA, Transfer, His/chemistry/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Substrate Specificity
RF  - 264
EDAT- 1999/08/03 00:00
MHDA- 1999/08/03 00:01
CRDT- 1999/08/03 00:00
PHST- 1999/08/03 00:00 [pubmed]
PHST- 1999/08/03 00:01 [medline]
PHST- 1999/08/03 00:00 [entrez]
AID - 10.1515/BC.1999.079 [doi]
PST - ppublish
SO  - Biol Chem. 1999 Jun;380(6):623-46. doi: 10.1515/BC.1999.079.