2fca: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(10 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2fca.gif|left|200px]]


<!--
==The structure of BsTrmB==
The line below this paragraph, containing "STRUCTURE_2fca", creates the "Structure Box" on the page.
<StructureSection load='2fca' size='340' side='right'caption='[[2fca]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2fca]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FCA FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
{{STRUCTURE_2fca| PDB=2fca |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fca OCA], [https://pdbe.org/2fca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fca RCSB], [https://www.ebi.ac.uk/pdbsum/2fca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fca ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRMB_BACSU TRMB_BACSU] Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.[HAMAP-Rule:MF_01057]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fc/2fca_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fca ConSurf].
<div style="clear:both"></div>


'''The structure of BsTrmB'''
==See Also==
 
*[[TRNA methyltransferase 3D structures|TRNA methyltransferase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The structure of Bacillus subtilis TrmB (BsTrmB), the tRNA (m7G46) methyltransferase, was determined at a resolution of 2.1 A. This is the first structure of a member of the TrmB family to be determined by X-ray crystallography. It reveals a unique variant of the Rossmann-fold methyltransferase (RFM) structure, with the N-terminal helix folded on the opposite site of the catalytic domain. The architecture of the active site and a computational docking model of BsTrmB in complex with the methyl group donor S-adenosyl-L-methionine and the tRNA substrate provide an explanation for results from mutagenesis studies of an orthologous enzyme from Escherichia coli (EcTrmB). However, unlike EcTrmB, BsTrmB is shown here to be dimeric both in the crystal and in solution. The dimer interface has a hydrophobic core and buries a potassium ion and five water molecules. The evolutionary analysis of the putative interface residues in the TrmB family suggests that homodimerization may be a specific feature of TrmBs from Bacilli, which may represent an early stage of evolution to an obligatory dimer.
 
==About this Structure==
2FCA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FCA OCA].
 
==Reference==
Crystal structure of Bacillus subtilis TrmB, the tRNA (m7G46) methyltransferase., Zegers I, Gigot D, van Vliet F, Tricot C, Aymerich S, Bujnicki JM, Kosinski J, Droogmans L, Nucleic Acids Res. 2006 Apr 5;34(6):1925-34. Print 2006. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16600901 16600901]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bujnicki, J.]]
[[Category: Bujnicki J]]
[[Category: Droogmans, L.]]
[[Category: Droogmans L]]
[[Category: Gigot, D.]]
[[Category: Gigot D]]
[[Category: Kosinski, J.]]
[[Category: Kosinski J]]
[[Category: Vliet, F Van.]]
[[Category: Van Vliet F]]
[[Category: Zegers, I.]]
[[Category: Zegers I]]
[[Category: Methyltransferase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:43:11 2008''

Latest revision as of 12:22, 14 February 2024

The structure of BsTrmBThe structure of BsTrmB

Structural highlights

2fca is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRMB_BACSU Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.[HAMAP-Rule:MF_01057]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2fca, resolution 2.10Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA