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1kwg

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[[Image:1kwg.gif|left|200px]]
 
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{{Structure
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==Crystal structure of Thermus thermophilus A4 beta-galactosidase==
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|PDB= 1kwg |SIZE=350|CAPTION= <scene name='initialview01'>1kwg</scene>, resolution 1.60&Aring;
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<StructureSection load='1kwg' size='340' side='right'caption='[[1kwg]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
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<table><tr><td colspan='2'>[[1kwg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KWG FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23]
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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]] 1.6&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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}}
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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=1kwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kwg OCA], [https://pdbe.org/1kwg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kwg RCSB], [https://www.ebi.ac.uk/pdbsum/1kwg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kwg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BGAL_THETH BGAL_THETH]
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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/kw/1kwg_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=1kwg ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of Thermus thermophilus A4 beta-galactosidase'''
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==See Also==
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*[[Galactosidase 3D structures|Galactosidase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The beta-galactosidase from an extreme thermophile, Thermus thermophilus A4 (A4-beta-Gal), is thermostable and belongs to the glycoside hydrolase family 42 (GH-42). As the first known structures of a GH-42 enzyme, we determined the crystal structures of free and galactose-bound A4-beta-Gal at 1.6A and 2.2A resolution, respectively. A4-beta-Gal forms a homotrimeric structure resembling a flowerpot. Each monomer has an active site located inside a large central tunnel. The N-terminal domain of A4-beta-Gal has a TIM barrel fold, as predicted from hydrophobic cluster analysis. The putative catalytic residues of A4-beta-Gal (Glu141 and Glu312) superimpose well with the catalytic residues of Escherichia coli beta-galactosidase. The environment around the catalytic nucleophile (Glu312) is similar to that in the case of E.coli beta-galactosidase, but the recognition mechanism for a substrate is different. Trp182 of the next subunit of the trimer constitutes a part of the active-site pocket, indicating that the trimeric structure is essential for the enzyme activity. Structural comparison with other glycoside hydrolases revealed that many features of the 4/7 superfamily are conserved in the A4-beta-Gal structure. On the basis of the results of 1H NMR spectroscopy, A4-beta-Gal was determined to be a "retaining" enzyme. Interestingly, the active site was similar with those of retaining enzymes, but the overall fold of the TIM barrel domain was very similar to that of an inverting enzyme, beta-amylase.
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[[Category: Large Structures]]
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==About this Structure==
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1KWG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KWG OCA].
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==Reference==
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Trimeric crystal structure of the glycoside hydrolase family 42 beta-galactosidase from Thermus thermophilus A4 and the structure of its complex with galactose., Hidaka M, Fushinobu S, Ohtsu N, Motoshima H, Matsuzawa H, Shoun H, Wakagi T, J Mol Biol. 2002 Sep 6;322(1):79-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12215416 12215416]
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[[Category: Beta-galactosidase]]
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[[Category: Single protein]]
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[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: Fushinobu, S.]]
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[[Category: Fushinobu S]]
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[[Category: Hidaka, M.]]
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[[Category: Hidaka M]]
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[[Category: Matsuzawa, H.]]
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[[Category: Matsuzawa H]]
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[[Category: Motoshima, H.]]
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[[Category: Motoshima H]]
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[[Category: Ohtsu, N.]]
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[[Category: Ohtsu N]]
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[[Category: Shoun, H.]]
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[[Category: Shoun H]]
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[[Category: Wakagi, T.]]
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[[Category: Wakagi T]]
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[[Category: ACT]]
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[[Category: CL]]
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[[Category: MPD]]
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[[Category: ZN]]
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[[Category: glycoside hydrolase family 42]]
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[[Category: tim barrel]]
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[[Category: trimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:23:08 2008''
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Current revision

Crystal structure of Thermus thermophilus A4 beta-galactosidase

PDB ID 1kwg

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