1b1a

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(New page: 200px<br /><applet load="1b1a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b1a" /> '''GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR,...)
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[[Image:1b1a.gif|left|200px]]<br /><applet load="1b1a" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1b1a" />
 
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'''GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR, MINIMIZED AVERAGE STRUCTURE'''<br />
 
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==Overview==
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==GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR, MINIMIZED AVERAGE STRUCTURE==
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Glutamate mutase (Glm) is an adenosylcobamide-dependent enzyme that, catalyzes the reversible rearrangement of (2S)-glutamate to (2S, 3S)-3-methylaspartate. The active enzyme from Clostridium cochlearium, consists of two subunits (of 53.6 and 14.8 kDa) as an alpha2beta2, tetramer, whose assembly is mediated by coenzyme B12. The smaller of the, protein components, GlmS, has been suggested to be the B12-binding, subunit. Here we report the solution structure of GlmS, determined from a, heteronuclear NMR-study, and the analysis of important dynamical aspects, of this apoenzyme subunit. The global fold and dynamic behavior of GlmS in, solution are similar to those of the corresponding subunit MutS from C., tetanomorphum, which has previously been investigated using, NMR-spectroscopy. Both solution structures of the two Glm B12-binding, subunits share striking similarities with that determined by, crystallography for the B12-binding domain of methylmalonyl CoA mutase, (Mcm) from Propionibacterium shermanii, which is B12 bound. In the crystal, structure a conserved histidine residue was found to be coordinated to, cobalt, displacing the endogenous axial ligand of the cobamide. However, in GlmS and MutS the sequence motif, Asp-x-His-x-x-Gly, which includes the, cobalt-coordinating histidine residue, and a predicted alpha-helical, region following the motif, are present as an unstructured and highly, mobile loop. In the absence of coenzyme, the B12-binding site apparently, is only partially formed. By comparing the crystal structure of Mcm with, the solution structures of B12-free GlmS and MutS, a consistent picture on, the mechanism of B12 binding has been obtained. Important elements of the, binding site only become structured upon binding B12; these include the, cobalt-coordinating histidine residue, and an alpha helix that forms one, side of the cleft accommodating the nucleotide 'tail' of the coenzyme.
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<StructureSection load='1b1a' size='340' side='right'caption='[[1b1a]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1b1a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_cochlearium Clostridium cochlearium]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B1A FirstGlance]. <br>
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1B1A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_cochlearium Clostridium cochlearium]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B1A OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1b1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b1a OCA], [https://pdbe.org/1b1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b1a RCSB], [https://www.ebi.ac.uk/pdbsum/1b1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b1a ProSAT]</span></td></tr>
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==Reference==
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</table>
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Structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium cochlearium., Hoffmann B, Konrat R, Bothe H, Buckel W, Krautler B, Eur J Biochem. 1999 Jul;263(1):178-88. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10429202 10429202]
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== Function ==
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[https://www.uniprot.org/uniprot/GMSS_CLOCO GMSS_CLOCO] Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).[HAMAP-Rule:MF_00526]<ref>PMID:1315276</ref> <ref>PMID:7880251</ref> <ref>PMID:8013871</ref>
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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/b1/1b1a_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=1b1a ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Clostridium cochlearium]]
[[Category: Clostridium cochlearium]]
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[[Category: Methylaspartate mutase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Bothe H]]
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[[Category: Bothe, H.]]
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[[Category: Buckel W]]
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[[Category: Buckel, W.]]
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[[Category: Hoffmann B]]
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[[Category: Hoffmann, B.]]
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[[Category: Konrat R]]
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[[Category: Konrat, R.]]
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[[Category: Kraeutler B]]
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[[Category: Kraeutler, B.]]
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[[Category: b12-binding subunit]]
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[[Category: glutamate mutase]]
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[[Category: isomerase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:16:42 2007''
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Current revision

GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR, MINIMIZED AVERAGE STRUCTURE

PDB ID 1b1a

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