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1eh9

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[[Image:1eh9.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF SULFOLOBUS SOLFATARICUS GLYCOSYLTREHALOSE TREHALOHYDROLASE==
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|PDB= 1eh9 |SIZE=350|CAPTION= <scene name='initialview01'>1eh9</scene>, resolution 3.0&Aring;
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<StructureSection load='1eh9' size='340' side='right'caption='[[1eh9]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1eh9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EH9 FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] </span>
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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]] 3&#8491;</td></tr>
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|GENE=
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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=1eh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eh9 OCA], [https://pdbe.org/1eh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eh9 RCSB], [https://www.ebi.ac.uk/pdbsum/1eh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eh9 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1eha|1EHA]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eh9 OCA], [http://www.ebi.ac.uk/pdbsum/1eh9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eh9 RCSB]</span>
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[https://www.uniprot.org/uniprot/TREZ_SACSO TREZ_SACSO]
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''CRYSTAL STRUCTURE OF SULFOLOBUS SOLFATARICUS GLYCOSYLTREHALOSE TREHALOHYDROLASE'''
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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/eh/1eh9_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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The crystal structure of glycosyltrehalose trehalohydrolase from the hyperthermophilic archaeum Sulfolobus solfataricus KM1 has been solved by multiple isomorphous replacement. The enzyme is an alpha-amylase (family 13) with unique exo-amylolytic activity for glycosyltrehalosides. It cleaves the alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose and maltooligo saccharide. Unlike most other family 13 glycosidases, the enzyme does not require Ca(2+) for activity, and it contains an N-terminal extension of approximately 100 amino acid residues that is homologous to N-terminal domains found in many glycosidases that recognize branched oligosaccharides. Crystallography revealed the enzyme to exist as a homodimer covalently linked by an intermolecular disulfide bond at residue C298. The existence of the intermolecular disulfide bond was confirmed by biochemical analysis and mutagenesis. The N-terminal extension forms an independent domain connected to the catalytic domain by an extended linker. The functionally essential Ca(2+) binding site found in the B domain of alpha-amylases and many other family 13 glycosidases was found to be replaced by hydrophobic packing interactions. The enzyme also contains a very unusual excursion in the (beta/alpha)(8) barrel structure of the catalytic domain. This excursion originates from the bottom of the (beta/alpha)(8) barrel between helix 6 and strand 7, but folds upward in a distorted alpha-hairpin structure to form a part of the substrate binding cleft wall that is possibly critical for the enzyme's unique substrate selectivity. Participation of an alpha-beta loop in the formation of the substrate binding cleft is a novel feature that is not observed in other known (beta/alpha)(8) enzymes.
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==About this Structure==
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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=1eh9 ConSurf].
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1EH9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EH9 OCA].
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<div style="clear:both"></div>
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of glycosyltrehalose trehalohydrolase from the hyperthermophilic archaeum Sulfolobus solfataricus., Feese MD, Kato Y, Tamada T, Kato M, Komeda T, Miura Y, Hirose M, Hondo K, Kobayashi K, Kuroki R, J Mol Biol. 2000 Aug 11;301(2):451-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10926520 10926520]
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[[Category: Large Structures]]
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[[Category: Alpha-amylase]]
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[[Category: Saccharolobus solfataricus]]
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[[Category: Single protein]]
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[[Category: Feese MD]]
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[[Category: Sulfolobus solfataricus]]
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[[Category: Kato M]]
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[[Category: Feese, M D.]]
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[[Category: Kato Y]]
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[[Category: Kato, M.]]
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[[Category: Kobayashi K]]
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[[Category: Kato, Y.]]
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[[Category: Komeda T]]
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[[Category: Kobayashi, K.]]
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[[Category: Kuroki R]]
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[[Category: Komeda, T.]]
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[[Category: Tamada T]]
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[[Category: Kuroki, R.]]
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[[Category: Tamada, T.]]
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[[Category: alpha/beta barrel]]
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[[Category: calcium binding]]
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[[Category: covalent dimer]]
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[[Category: crystal structure]]
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[[Category: sulfolobus solfataricus]]
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[[Category: trehalohydrolase]]
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[[Category: trehalose]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:02:33 2008''
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Current revision

CRYSTAL STRUCTURE OF SULFOLOBUS SOLFATARICUS GLYCOSYLTREHALOSE TREHALOHYDROLASE

PDB ID 1eh9

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