1ual: Difference between revisions
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene> | |LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/tRNA_(guanine-N(1)-)-methyltransferase tRNA (guanine-N(1)-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.31 2.1.1.31] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/tRNA_(guanine-N(1)-)-methyltransferase tRNA (guanine-N(1)-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.31 2.1.1.31] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1uaj|1UAJ]], [[1uak|1UAK]], [[1uam|1UAM]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ual FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ual OCA], [http://www.ebi.ac.uk/pdbsum/1ual PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ual RCSB]</span> | |||
}} | }} | ||
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[[Category: Yang, J K.]] | [[Category: Yang, J K.]] | ||
[[Category: Yoon, H J.]] | [[Category: Yoon, H J.]] | ||
[[Category: methyltransferase]] | [[Category: methyltransferase]] | ||
[[Category: spout class]] | [[Category: spout class]] | ||
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[[Category: trna(m1g37)methyltransferase]] | [[Category: trna(m1g37)methyltransferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:07:39 2008'' | ||
Revision as of 21:07, 30 March 2008
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| 1ual, resolution 1.80Å | |||||||||||||
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| Ligands: | SAH | ||||||||||||
| Activity: | tRNA (guanine-N(1)-)-methyltransferase, with EC number 2.1.1.31 | ||||||||||||
| Related: | 1UAJ, 1UAK, 1UAM
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal structure of tRNA(m1G37)methyltransferase: Insight into tRNA recognition
Overview
tRNA(m(1)G37)methyltransferase (TrmD) catalyzes the transfer of a methyl group from S-adenosyl-L- methionine (AdoMet) to G(37) within a subset of bacterial tRNA species, which have a G residue at the 36th position. The modified guanosine is adjacent to and 3' of the anticodon and is essential for the maintenance of the correct reading frame during translation. Here we report four crystal structures of TrmD from Haemophilus influenzae, as binary complexes with either AdoMet or S-adenosyl-L-homocysteine (AdoHcy), as a ternary complex with AdoHcy and phosphate, and as an apo form. This first structure of TrmD indicates that it functions as a dimer. It also suggests the binding mode of G(36)G(37) in the active site of TrmD and the catalytic mechanism. The N-terminal domain has a trefoil knot, in which AdoMet or AdoHcy is bound in a novel, bent conformation. The C-terminal domain shows structural similarity to trp repressor. We propose a plausible model for the TrmD(2)-tRNA(2) complex, which provides insights into recognition of the general tRNA structure by TrmD.
About this Structure
1UAL is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition., Ahn HJ, Kim HW, Yoon HJ, Lee BI, Suh SW, Yang JK, EMBO J. 2003 Jun 2;22(11):2593-603. PMID:12773376
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