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== Histidyl-tRNA Synthetase == | == Histidyl-tRNA Synthetase == | ||
| - | Histidyl tRNA Synthetase (HisRS) is a 94kD <scene name='User:Jamie_Abbott/Sandbox2/Hisrsdimer/2'>homodimer</scene> that belongs to the Class II of aminoacyl-tRNA synthetases (aaRS). Aminoacyl-tRNA synthetases have been partitioned into two classes on the basis of sequence<ref>PMID: 2203971</ref>. Class II enzymes have a <scene name='User:Jamie_Abbott/Sandbox2/Catalytic_domain/1'>catalytic domain</scene> composed of anti-parallel β-sheets and α-helices (residues 1-325). | + | Histidyl tRNA Synthetase (HisRS) is a 94kD <scene name='User:Jamie_Abbott/Sandbox2/Hisrsdimer/2'>homodimer</scene> that belongs to the Class II of aminoacyl-tRNA synthetases (aaRS). Aminoacyl-tRNA synthetases have been partitioned into two classes, containing 10 members, on the basis of sequence comparisons<ref name="Eriani">PMID: 2203971</ref>. ClassI and Class II differ mainly with respect to the topology of the catalytic fold and site of esterification on cognate tRNA<ref name="Eriani" />. Class II enzymes have a <scene name='User:Jamie_Abbott/Sandbox2/Catalytic_domain/1'>catalytic domain</scene> composed of anti-parallel β-sheets and α-helices (residues 1-325). |
'''Function and Catalysis'''<StructureSection load='1KMM' size='500' side='right' caption='Structure of Histidyl-tRNA Synthetase (PDB entry [[1KMM]])' scene=''>Class II aminoacyl-tRNA synthetases aminoacylate the 3'OH of their cognate tRNAs. | '''Function and Catalysis'''<StructureSection load='1KMM' size='500' side='right' caption='Structure of Histidyl-tRNA Synthetase (PDB entry [[1KMM]])' scene=''>Class II aminoacyl-tRNA synthetases aminoacylate the 3'OH of their cognate tRNAs. | ||
Revision as of 21:05, 14 April 2012
Contents |
Histidyl-tRNA Synthetase
Histidyl tRNA Synthetase (HisRS) is a 94kD that belongs to the Class II of aminoacyl-tRNA synthetases (aaRS). Aminoacyl-tRNA synthetases have been partitioned into two classes, containing 10 members, on the basis of sequence comparisons[1]. ClassI and Class II differ mainly with respect to the topology of the catalytic fold and site of esterification on cognate tRNA[1]. Class II enzymes have a composed of anti-parallel β-sheets and α-helices (residues 1-325).
Function and Catalysis
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Mechanism
3D Structures of Histidyl-tRNA Synthetase
References
- ↑ 1.0 1.1 Eriani G, Delarue M, Poch O, Gangloff J, Moras D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature. 1990 Sep 13;347(6289):203-6. PMID:2203971 doi:http://dx.doi.org/10.1038/347203a0
- ↑ 2.0 2.1 Francklyn, C., and Arnez, J.G. (2004) in Aminoacyl-tRNA Synthetases (Ibba, M.,Francklyn, C.,Cusack, S.. Eds.) Landes Publishing, Austin, TX
