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[[Image:1k98.jpg|left|200px]]
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{{STRUCTURE_1k98|  PDB=1k98  |  SCENE=  }}
'''AdoMet complex of MetH C-terminal fragment'''


==AdoMet complex of MetH C-terminal fragment==
<StructureSection load='1k98' size='340' side='right'caption='[[1k98]], [[Resolution|resolution]] 3.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1k98]] 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=1K98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K98 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]] 3.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1k98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k98 OCA], [https://pdbe.org/1k98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k98 RCSB], [https://www.ebi.ac.uk/pdbsum/1k98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k98 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/METH_ECOLI METH_ECOLI] Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
== 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/k9/1k98_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1k98 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
B(12)-dependent methionine synthase (MetH) from Escherichia coli is a large modular protein that uses bound cobalamin as an intermediate methyl carrier. Major domain rearrangements have been postulated to explain how cobalamin reacts with three different substrates: homocysteine, methyltetrahydrofolate and S-adenosylmethionine (AdoMet). Here we describe the 3.0 A structure of a 65 kDa C-terminal fragment of MetH that spans the cobalamin- and AdoMet-binding domains, arranged in a conformation suitable for the methyl transfer from AdoMet to cobalamin that occurs during activation. In the conversion to the activation conformation, a helical domain that capped the cofactor moves 26 A and rotates by 63 degrees, allowing formation of a new interface between cobalamin and the AdoMet-binding (activation) domain. Interactions with the MetH activation domain drive the cobalamin away from its binding domain in a way that requires dissociation of the axial cobalt ligand and, thereby, provide a mechanism for control of the distribution of enzyme conformations.


==Overview==
Domain alternation switches B(12)-dependent methionine synthase to the activation conformation.,Bandarian V, Pattridge KA, Lennon BW, Huddler DP, Matthews RG, Ludwig ML Nat Struct Biol. 2002 Jan;9(1):53-6. PMID:11731805<ref>PMID:11731805</ref>
B(12)-dependent methionine synthase (MetH) from Escherichia coli is a large modular protein that uses bound cobalamin as an intermediate methyl carrier. Major domain rearrangements have been postulated to explain how cobalamin reacts with three different substrates: homocysteine, methyltetrahydrofolate and S-adenosylmethionine (AdoMet). Here we describe the 3.0 A structure of a 65 kDa C-terminal fragment of MetH that spans the cobalamin- and AdoMet-binding domains, arranged in a conformation suitable for the methyl transfer from AdoMet to cobalamin that occurs during activation. In the conversion to the activation conformation, a helical domain that capped the cofactor moves 26 A and rotates by 63 degrees, allowing formation of a new interface between cobalamin and the AdoMet-binding (activation) domain. Interactions with the MetH activation domain drive the cobalamin away from its binding domain in a way that requires dissociation of the axial cobalt ligand and, thereby, provide a mechanism for control of the distribution of enzyme conformations.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1K98 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K98 OCA].
</div>
<div class="pdbe-citations 1k98" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Domain alternation switches B(12)-dependent methionine synthase to the activation conformation., Bandarian V, Pattridge KA, Lennon BW, Huddler DP, Matthews RG, Ludwig ML, Nat Struct Biol. 2002 Jan;9(1):53-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11731805 11731805]
*[[Methionine synthase 3D structures|Methionine synthase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Methionine synthase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Bandarian V]]
[[Category: Bandarian, V.]]
[[Category: Huddler DP]]
[[Category: Huddler, D P.]]
[[Category: Lennon BW]]
[[Category: Lennon, B W.]]
[[Category: Ludwig ML]]
[[Category: Ludwig, M L.]]
[[Category: Matthews RG]]
[[Category: Matthews, R G.]]
[[Category: Pattridge KA]]
[[Category: Pattridge, K A.]]
[[Category: Adomet binding]]
[[Category: Domain interaction]]
[[Category: Motion of 4-helix bundle]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:27:47 2008''
Retrieved from "https://proteopedia.org/1k98"