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1qvb

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[[Image:1qvb.jpg|left|200px]]
 
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==CRYSTAL STRUCTURE OF THE BETA-GLYCOSIDASE FROM THE HYPERTHERMOPHILE THERMOSPHAERA AGGREGANS==
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The line below this paragraph, containing "STRUCTURE_1qvb", creates the "Structure Box" on the page.
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<StructureSection load='1qvb' size='340' side='right'caption='[[1qvb]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1qvb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosphaera_aggregans Thermosphaera aggregans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QVB FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.4&#8491;</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=1qvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qvb OCA], [https://pdbe.org/1qvb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qvb RCSB], [https://www.ebi.ac.uk/pdbsum/1qvb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qvb ProSAT]</span></td></tr>
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{{STRUCTURE_1qvb| PDB=1qvb | SCENE= }}
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</table>
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== Function ==
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'''CRYSTAL STRUCTURE OF THE BETA-GLYCOSIDASE FROM THE HYPERTHERMOPHILE THERMOSPHAERA AGGREGANS'''
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[https://www.uniprot.org/uniprot/Q9YGA8_9CREN Q9YGA8_9CREN]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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The glycosyl hydrolases are an important group of enzymes that are responsible for cleaving a range of biologically significant carbohydrate compounds. Structural information on these enzymes has provided useful information on their molecular basis for the functional variations, while the characterization of the structural features that account for the high thermostability of proteins is of great scientific and biotechnological interest. To these ends we have determined the crystal structure of the beta-glycosidase from a hyperthermophilic archeon Thermosphaera aggregans. The structure is a (beta/alpha)8 barrel (TIM-barrel), as seen in other glycosyl hydrolase family 1 members, and forms a tetramer. Inspection of the active site and the surrounding area reveals two catalytic glutamate residues consistent with the retaining mechanism and the surrounding polar and aromatic residues consistent with a monosaccharide binding site. Comparison of this structure with its mesophilic counterparts implicates a variety of structural features that could contribute to the thermostability. These include an increased number of surface ion pairs, an increased number of internal water molecules and a decreased surface area upon forming an oligomeric quaternary structure.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qv/1qvb_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1QVB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermosphaera_aggregans Thermosphaera aggregans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QVB OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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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=1qvb ConSurf].
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Crystal structure of the beta-glycosidase from the hyperthermophile Thermosphaera aggregans: insights into its activity and thermostability., Chi YI, Martinez-Cruz LA, Jancarik J, Swanson RV, Robertson DE, Kim SH, FEBS Lett. 1999 Feb 26;445(2-3):375-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10094493 10094493]
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<div style="clear:both"></div>
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[[Category: Single protein]]
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Thermosphaera aggregans]]
[[Category: Thermosphaera aggregans]]
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[[Category: Chi, Y I.]]
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[[Category: Chi Y-I]]
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[[Category: Kim, S H.]]
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[[Category: Kim S-H]]
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[[Category: Martinez-Cruz, L A.]]
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[[Category: Martinez-Cruz LA]]
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[[Category: Robertson, D E.]]
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[[Category: Robertson DE]]
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[[Category: Swanson, R V.]]
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[[Category: Swanson RV]]
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[[Category: Thermostable]]
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[[Category: Tim-barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:44:35 2008''
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Current revision

CRYSTAL STRUCTURE OF THE BETA-GLYCOSIDASE FROM THE HYPERTHERMOPHILE THERMOSPHAERA AGGREGANS

PDB ID 1qvb

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