1xrc: Difference between revisions

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New page: left|200px<br /><applet load="1xrc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xrc, resolution 3.0Å" /> '''CRYSTAL STRUCTURE OF ...
 
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'''CRYSTAL STRUCTURE OF S-ADENOSYLMETHIONINE SYNTHETASE'''<br />


==Overview==
==CRYSTAL STRUCTURE OF S-ADENOSYLMETHIONINE SYNTHETASE==
The structure of S-adenosylmethionine synthetase (MAT, ATP:L-methionine, S-adenosyltransferase, EC 2.5.1.6.) from Escherichia coli has been, determined at 3.0 A resolution by multiple isomorphous replacement using a, uranium derivative and the selenomethionine form of the enzyme (SeMAT)., The SeMAT data (9 selenomethionine residues out of 383 amino acid, residues) have been found to have a sufficient phasing power to determine, the structure of the 42,000 molecular weight protein by combining them, with the other heavy atom derivative data (multiple isomorphous, replacement). The enzyme consists of four identical subunits; two subunits, form a spherical tight dimer, and pairs of these dimers form a, peanut-shaped tetrameric enzyme. Each pair dimer has two active sites, which are located between the subunits. Each subunit consists of three, domains that are related to each other by pseudo-3-fold symmetry. The, essential divalent (Mg2+/Co2+) and monovalent (K+) metal ions and one of, the product, Pi ions, were found in the active site from three separate, structures.
<StructureSection load='1xrc' size='340' side='right'caption='[[1xrc]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1xrc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XRC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=1xrc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrc OCA], [https://pdbe.org/1xrc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xrc RCSB], [https://www.ebi.ac.uk/pdbsum/1xrc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xrc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/METK_ECOLI METK_ECOLI] Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. Is essential for growth.[HAMAP-Rule:MF_00086]
== 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/xr/1xrc_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=1xrc ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1XRC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4, CO and K as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.6 2.5.1.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XRC OCA].
*[[S-adenosylmethionine synthetase 3D structures|S-adenosylmethionine synthetase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of S-adenosylmethionine synthetase., Takusagawa F, Kamitori S, Misaki S, Markham GD, J Biol Chem. 1996 Jan 5;271(1):136-47. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8550549 8550549]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Methionine adenosyltransferase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Kamitori S]]
[[Category: Kamitori, S.]]
[[Category: Markham GD]]
[[Category: Markham, G.D.]]
[[Category: Misaki S]]
[[Category: Misaki, S.]]
[[Category: Takusagawa F]]
[[Category: Takusagawa, F.]]
[[Category: CO]]
[[Category: K]]
[[Category: PO4]]
[[Category: methyltransferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:17:16 2007''

Latest revision as of 11:52, 14 February 2024

CRYSTAL STRUCTURE OF S-ADENOSYLMETHIONINE SYNTHETASECRYSTAL STRUCTURE OF S-ADENOSYLMETHIONINE SYNTHETASE

Structural highlights

1xrc is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

METK_ECOLI Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. Is essential for growth.[HAMAP-Rule:MF_00086]

Evolutionary Conservation

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

See Also

1xrc, resolution 3.00Å

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