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| <StructureSection load='1uaj' size='340' side='right'caption='[[1uaj]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='1uaj' size='340' side='right'caption='[[1uaj]], [[Resolution|resolution]] 1.85Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1uaj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UAJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UAJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1uaj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UAJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UAJ FirstGlance]. <br> |
- | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1uak|1uak]], [[1ual|1ual]], [[1uam|1uam]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.221 and 2.1.1.228 2.1.1.221 and 2.1.1.228] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uaj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uaj OCA], [https://pdbe.org/1uaj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uaj RCSB], [https://www.ebi.ac.uk/pdbsum/1uaj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uaj ProSAT]</span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uaj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uaj OCA], [http://pdbe.org/1uaj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uaj RCSB], [http://www.ebi.ac.uk/pdbsum/1uaj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1uaj ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/TRMD_HAEIN TRMD_HAEIN]] Specifically methylates guanosine-37 in various tRNAs (By similarity).[HAMAP-Rule:MF_00605] | + | [https://www.uniprot.org/uniprot/TRMD_HAEIN TRMD_HAEIN] Specifically methylates guanosine-37 in various tRNAs (By similarity).[HAMAP-Rule:MF_00605] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| ==See Also== | | ==See Also== |
- | *[[TRNA methyltransferase|TRNA methyltransferase]] | + | *[[TRNA methyltransferase 3D structures|TRNA methyltransferase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Bacterium influenzae lehmann and neumann 1896]] | + | [[Category: Haemophilus influenzae]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Transferase]]
| + | [[Category: Ahn HJ]] |
- | [[Category: Ahn, H J]] | + | [[Category: Kim H-W]] |
- | [[Category: Kim, H W]] | + | [[Category: Lee BI]] |
- | [[Category: Lee, B I]] | + | [[Category: Suh SW]] |
- | [[Category: Suh, S W]] | + | [[Category: Yang JK]] |
- | [[Category: Yang, J K]] | + | [[Category: Yoon H-J]] |
- | [[Category: Yoon, H J]] | + | |
- | [[Category: Methyltransferase]]
| + | |
- | [[Category: Spout class]]
| + | |
- | [[Category: Trmd]]
| + | |
- | [[Category: Trna modification]]
| + | |
| Structural highlights
Function
TRMD_HAEIN Specifically methylates guanosine-37 in various tRNAs (By similarity).[HAMAP-Rule:MF_00605]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ahn HJ, Kim HW, Yoon HJ, Lee BI, Suh SW, Yang JK. Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition. EMBO J. 2003 Jun 2;22(11):2593-603. PMID:12773376 doi:10.1093/emboj/cdg269
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