1k98

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(New page: 200px<br /><applet load="1k98" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k98, resolution 3.75&Aring;" /> '''AdoMet complex of Me...)
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[[Image:1k98.jpg|left|200px]]<br /><applet load="1k98" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1k98, resolution 3.75&Aring;" />
 
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'''AdoMet complex of MetH C-terminal fragment'''<br />
 
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==Overview==
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==AdoMet complex of MetH C-terminal fragment==
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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.
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<StructureSection load='1k98' size='340' side='right'caption='[[1k98]], [[Resolution|resolution]] 3.75&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k9/1k98_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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1K98 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 SO4 and B12 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Methionine_synthase Methionine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.13 2.1.1.13] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K98 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11731805 11731805]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 1k98" style="background-color:#fffaf0;"></div>
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[[Category: Methionine synthase]]
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[[Category: Single protein]]
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[[Category: Bandarian, V.]]
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[[Category: Huddler, D.P.]]
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[[Category: Lennon, B.W.]]
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[[Category: Ludwig, M.L.]]
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[[Category: Matthews, R.G.]]
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[[Category: Pattridge, K.A.]]
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[[Category: B12]]
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[[Category: SO4]]
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[[Category: adomet binding]]
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[[Category: domain interactions]]
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[[Category: motion of 4-helix bundle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:58:19 2007''
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==See Also==
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*[[Methionine synthase 3D structures|Methionine synthase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Bandarian V]]
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[[Category: Huddler DP]]
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[[Category: Lennon BW]]
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[[Category: Ludwig ML]]
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[[Category: Matthews RG]]
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[[Category: Pattridge KA]]

Current revision

AdoMet complex of MetH C-terminal fragment

PDB ID 1k98

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