1i9c: Difference between revisions

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[[Image:1i9c.jpg|left|200px]]


{{Structure
==GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM: COMPLEX WITH ADENOSYLCOBALAMIN AND SUBSTRATE==
|PDB= 1i9c |SIZE=350|CAPTION= <scene name='initialview01'>1i9c</scene>, resolution 1.90&Aring;
<StructureSection load='1i9c' size='340' side='right'caption='[[1i9c]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=5AD:5&#39;-DEOXYADENOSINE'>5AD</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene> and <scene name='pdbligand=3MD:2S,3S-3-METHYLASPARTIC ACID'>3MD</scene>
<table><tr><td colspan='2'>[[1i9c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_cochlearium Clostridium cochlearium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I9C 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">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE= GLMS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1494 Clostridium cochlearium]), GLME ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1494 Clostridium cochlearium])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2AS:(2S,3S)-3-METHYL-ASPARTIC+ACID'>2AS</scene>, <scene name='pdbligand=5AD:5-DEOXYADENOSINE'>5AD</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</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=1i9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9c OCA], [https://pdbe.org/1i9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i9c RCSB], [https://www.ebi.ac.uk/pdbsum/1i9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i9c ProSAT]</span></td></tr>
 
</table>
'''GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM: COMPLEX WITH ADENOSYLCOBALAMIN AND SUBSTRATE'''
== Function ==
 
[https://www.uniprot.org/uniprot/GLME_CLOCO GLME_CLOCO] Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).<ref>PMID:7880251</ref> <ref>PMID:1315276</ref>
 
== Evolutionary Conservation ==
==About this Structure==
[[Image:Consurf_key_small.gif|200px|right]]
1I9C is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Clostridium_cochlearium Clostridium cochlearium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I9C OCA].  
Check<jmol>
 
  <jmolCheckbox>
==Reference==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i9/1i9c_consurf.spt"</scriptWhenChecked>
Radical Shuttling in a Protein: Ribose Pseudorotation Controls Alkyl-Radical Transfer in the Coenzyme B(12) Dependent Enzyme Glutamate Mutase This work was supported by the Osterreichische Akademie der Wissenschaften (APART fellowship 614), the Osterreichische Fonds zur Forderung der wissenschaftlichen Forschung (FWF-project 11599), and the European Commission (TMR project number ERB 4061 PL 95-0307). Crystallographic data were collected at the EMBL-beamline BW7B at DESY in Hamburg, Germany. We thank the beamline scientists for their assistance, and Ingrid Dreveny, Gunter Gartler, Gerwald Jogl, and Oliver Sauer for their help during data collection. This research emerged from a collaboration with Prof. W. Buckel (Marburg) who supplied us with clones of the glutamate mutase proteins. , Gruber K, Reitzer R, Kratky C, Angew Chem Int Ed Engl. 2001 Sep 17;40(18):3377-3380. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11592143 11592143]
    <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=1i9c ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridium cochlearium]]
[[Category: Clostridium cochlearium]]
[[Category: Methylaspartate mutase]]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Gruber K]]
[[Category: Gruber, K.]]
[[Category: Kratky C]]
[[Category: Kratky, C.]]
[[Category: 3MD]]
[[Category: 5AD]]
[[Category: B12]]
[[Category: GLU]]
[[Category: coenzyme b12]]
[[Category: radical reaction]]
[[Category: ribose pseudorotation]]
[[Category: rossman-fold]]
[[Category: tim-barrel]]
 
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Retrieved from "https://proteopedia.org/1i9c"