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[[Image:1fmf.gif|left|200px]]


{{Structure
==REFINED SOLUTION STRUCTURE OF THE (13C,15N-LABELED) B12-BINDING SUBUNIT OF GLUTAMATE MUTASE FROM CLOSTRIDIUM TETANOMORPHUM==
|PDB= 1fmf |SIZE=350|CAPTION= <scene name='initialview01'>1fmf</scene>
<StructureSection load='1fmf' size='340' side='right'caption='[[1fmf]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1fmf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_tetanomorphum Clostridium tetanomorphum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FMF FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Methylaspartate_mutase Methylaspartate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.1 5.4.99.1]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fmf OCA], [https://pdbe.org/1fmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fmf RCSB], [https://www.ebi.ac.uk/pdbsum/1fmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fmf ProSAT]</span></td></tr>
}}
</table>
 
== Function ==
'''REFINED SOLUTION STRUCTURE OF THE (13C,15N-LABELED) B12-BINDING SUBUNIT OF GLUTAMATE MUTASE FROM CLOSTRIDIUM TETANOMORPHUM'''
[https://www.uniprot.org/uniprot/GMSS_CLOTT GMSS_CLOTT] Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).[HAMAP-Rule:MF_00526]<ref>PMID:8051138</ref>
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
==Overview==
Check<jmol>
Uniformly (13)C,(15)N-labeled MutS, the coenzyme B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum, was prepared by overexpression from an Escherichia coli strain. Multidimensional heteronuclear NMR spectroscopic experiments with aqueous solutions of (13)C,(15)N-labeled MutS provided signal assignments for roughly 90% of the 1025 hydrogen, 651 carbon, and 173 nitrogen atoms and resulted in about 1800 experimental restraints. Based on the information from the NMR experiments, the structure of MutS was calculated, confirming the earlier, less detailed structure obtained with (15)N-labeled MutS. The refined analysis allowed a precise determination of the secondary and tertiary structure including several crucial side chain interactions. The structures of (the apoprotein) MutS in solution and of the B(12)-binding subunit in the crystal of the corresponding homologous holoenzyme from Clostridium cochlearium differ only in a section that forms the well-structured helix alpha1 in the crystal structure and that also comprises the cobalt-coordinating histidine residue. In the apoprotein MutS, this part of the B(12)-binding subunit is dynamic. The carboxy-terminal end of this section is conformationally flexible and has significant propensity for an alpha-helical structure ("nascent helix"). This dynamic section in MutS is a decisive element for the binding of the nucleotide moiety of coenzyme B(12) and appears to be stabilized as a helix (alpha1) upon trapping of the nucleotide of the B(12) cofactor.
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/1fmf_consurf.spt"</scriptWhenChecked>
==About this Structure==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
1FMF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_tetanomorphum Clostridium tetanomorphum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMF OCA].  
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==Reference==
</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=1fmf ConSurf].
A protein pre-organized to trap the nucleotide moiety of coenzyme B(12): refined solution structure of the B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum., Hoffmann B, Tollinger M, Konrat R, Huhta M, Marsh EN, Krautler B, Chembiochem. 2001 Sep 3;2(9):643-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11828501 11828501]
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridium tetanomorphum]]
[[Category: Clostridium tetanomorphum]]
[[Category: Methylaspartate mutase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Hoffmann B]]
[[Category: Hoffmann, B.]]
[[Category: Huhta M]]
[[Category: Huhta, M]]
[[Category: Konrat R]]
[[Category: Konrat, R.]]
[[Category: Kraeutler B]]
[[Category: Kraeutler, B.]]
[[Category: Marsh ENG]]
[[Category: Marsh, E N.G.]]
[[Category: Tollinger M]]
[[Category: Tollinger, M.]]
[[Category: nucleotide binding fold]]
[[Category: rossmann fold]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:11:01 2008''

Latest revision as of 11:14, 27 March 2024

REFINED SOLUTION STRUCTURE OF THE (13C,15N-LABELED) B12-BINDING SUBUNIT OF GLUTAMATE MUTASE FROM CLOSTRIDIUM TETANOMORPHUM

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