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1lwh

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(New page: 200px<br /><applet load="1lwh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lwh, resolution 2.60&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1lwh.jpg|left|200px]]<br /><applet load="1lwh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lwh, resolution 2.60&Aring;" />
 
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'''CRYSTAL STRUCTURE OF T. MARITIMA 4-ALPHA-GLUCANOTRANSFERASE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF T. MARITIMA 4-ALPHA-GLUCANOTRANSFERASE==
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4-alpha-Glucanotransferase (GTase) is an essential enzyme in, alpha-1,4-glucan metabolism in bacteria and plants. It catalyses the, transfer of maltooligosaccharides from an 1,4-alpha-D-glucan molecule to, the 4-hydroxyl group of an acceptor sugar molecule. The crystal structures, of Thermotoga maritima GTase and its complex with the inhibitor acarbose, have been determined at 2.6A and 2.5A resolution, respectively. The GTase, structure consists of three domains, an N-terminal domain with the, (beta/alpha)(8) barrel topology (domain A), a 65 residue domain, domain B, inserted between strand beta3 and helix alpha6 of the barrel, and a, C-terminal domain, domain C, which forms an antiparallel beta-structure., Analysis of the complex of GTase with acarbose has revealed the locations, of five sugar-binding subsites (-2 to +3) in the active-site cleft lying, between domain B and the C-terminal end of the (beta/alpha)(8) barrel. The, structure of GTase closely resembles the family 13 glycoside hydrolases, and conservation of key catalytic residues previously identified for this, family is consistent with a double-displacement catalytic mechanism for, this enzyme. A distinguishing feature of GTase is a pair of tryptophan, residues, W131 and W218, which, upon the carbohydrate inhibitor binding, form a remarkable aromatic "clamp" that captures the sugar rings at the, acceptor-binding sites +1 and +2. Analysis of the structure of the complex, shows that sugar residues occupying subsites from -2 to +2 engage in, extensive interactions with the protein, whereas the +3 glucosyl residue, makes relatively few contacts with the enzyme. Thus, the structure, suggests that four subsites, from -2 to +2, play the dominant role in, enzyme-substrate recognition, consistent with the observation that the, smallest donor for T.maritima GTase is maltotetraose, the smallest chain, transferred is a maltosyl unit and that the smallest residual fragment, after transfer is maltose. A close similarity between the structures of, GTase and oligo-1,6-glucosidase has allowed the structural features that, determine differences in substrate specificity of these two enzymes to be, analysed.
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<StructureSection load='1lwh' size='340' side='right'caption='[[1lwh]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1lwh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LWH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LWH 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]] 2.6&#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=CA:CALCIUM+ION'>CA</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=1lwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lwh OCA], [https://pdbe.org/1lwh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lwh RCSB], [https://www.ebi.ac.uk/pdbsum/1lwh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lwh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MGTA_THEMA MGTA_THEMA]
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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/lw/1lwh_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=1lwh ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1LWH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/4-alpha-glucanotransferase 4-alpha-glucanotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.25 2.4.1.25] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LWH OCA].
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*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of Thermotoga maritima 4-alpha-glucanotransferase and its acarbose complex: implications for substrate specificity and catalysis., Roujeinikova A, Raasch C, Sedelnikova S, Liebl W, Rice DW, J Mol Biol. 2002 Aug 2;321(1):149-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12139940 12139940]
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[[Category: Large Structures]]
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[[Category: 4-alpha-glucanotransferase]]
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[[Category: Single protein]]
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Liebl, W.]]
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[[Category: Liebl W]]
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[[Category: Raasch, C.]]
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[[Category: Raasch C]]
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[[Category: Rice, D.W.]]
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[[Category: Rice DW]]
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[[Category: Roujeinikova, A.]]
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[[Category: Roujeinikova A]]
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[[Category: Sedelnikova, S.]]
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[[Category: Sedelnikova S]]
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[[Category: CA]]
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[[Category: 4-alpha-glucanotransferase]]
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[[Category: acarbose]]
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[[Category: alpha-amylase family]]
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[[Category: thermotoga maritima]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:56:18 2007''
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Current revision

CRYSTAL STRUCTURE OF T. MARITIMA 4-ALPHA-GLUCANOTRANSFERASE

PDB ID 1lwh

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