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<StructureSection load='1qvb' size='340' side='right'caption='[[1qvb]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1qvb' size='340' side='right'caption='[[1qvb]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1qvb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dsm_11486 Dsm 11486]. 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>
<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>
</td></tr><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>
</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>
<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>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9YGA8_9CREN Q9YGA8_9CREN]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:10094493<ref>PMID:10094493</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1qvb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Dsm 11486]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chi, Y I]]
[[Category: Thermosphaera aggregans]]
[[Category: Kim, S H]]
[[Category: Chi Y-I]]
[[Category: Martinez-Cruz, L A]]
[[Category: Kim S-H]]
[[Category: Robertson, D E]]
[[Category: Martinez-Cruz LA]]
[[Category: Swanson, R V]]
[[Category: Robertson DE]]
[[Category: Hydrolase]]
[[Category: Swanson RV]]
[[Category: Thermostable]]
[[Category: Tim-barrel]]

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