3ac0: Difference between revisions

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<StructureSection load='3ac0' size='340' side='right'caption='[[3ac0]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
<StructureSection load='3ac0' size='340' side='right'caption='[[3ac0]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ac0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cbs_712 Cbs 712]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AC0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ac0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_marxianus Kluyveromyces marxianus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AC0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene></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]] 2.54&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3abz|3abz]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Bgl, bglI ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4911 CBS 712])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] </span></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=3ac0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ac0 OCA], [https://pdbe.org/3ac0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ac0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ac0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ac0 ProSAT]</span></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=3ac0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ac0 OCA], [https://pdbe.org/3ac0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ac0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ac0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ac0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D1GCC6_KLUMA D1GCC6_KLUMA]
== 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=3ac0 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=3ac0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
beta-Glucosidase from Kluyveromyces marxianus (KmBglI) belongs to the glycoside hydrolase family 3 (GH3). The enzyme is particularly unusual in that a PA14 domain (pf07691), for which a carbohydrate-binding role has been claimed, is inserted into the catalytic core sequence. Here, we determined the enzymatic properties and crystal structure of KmBglI in complex with glucose at 2.55 A resolution. A striking characteristics of KmBglI was that the enzyme activity is essentially limited to disaccharides, and when trisaccharides were used as the substrates the activity was drastically decreased. This chain length specificity is in sharp contrast to the preferred action on oligosaccharides of barley beta-D-glucan glucohydrolase (ExoI), which does not have a PA14 domain insertion. The structure of subsite (-1) of KmBglI is almost identical to that of Thermotoga neapolitana beta-glucosidase and is also similar to that of ExoI, however, the structures of subsite (+1) significantly differ among them. In KmBglI, the loops extending from the PA14 domain cover the catalytic pocket to form subsite (+1), and hence simultaneously become a steric hindrance that could limit the chain length of the substrates to be accommodated. Mutational studies demonstrated the critical role of the loop regions in determining the substrate specificity. The active site formation mediated by the PA14 domain of KmBglI invokes alpha-complementation of beta-galactosidase exerted by its N-terminal domain, to which the PA14 domain shows structural resemblance. This is the first study that reveals the structural basis of the interaction between the PA14 domain and a carbohydrate.
Role of a PA14 domain in determining substrate specificity of a glycoside hydrolase family 3 beta-glucosidase from Kluyveromyces marxianus.,Yoshida E, Hidaka M, Fushinobu S, Koyanagi T, Minami H, Tamaki H, Kitaoka M, Katayama T, Kumagai H Biochem J. 2010 Jul 27. PMID:20662765<ref>PMID:20662765</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ac0" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Beta-glucosidase]]
[[Category: Kluyveromyces marxianus]]
[[Category: Cbs 712]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Fushinobu, S]]
[[Category: Fushinobu S]]
[[Category: Hidaka, M]]
[[Category: Hidaka M]]
[[Category: Katayama, T]]
[[Category: Katayama T]]
[[Category: Kumagai, H]]
[[Category: Kumagai H]]
[[Category: Yoshida, E]]
[[Category: Yoshida E]]
[[Category: Glycoside hydrolase family3 beta-glucosidase]]
[[Category: Hydrolase]]
[[Category: Pa14 domain]]

Latest revision as of 17:00, 13 March 2024

Crystal structure of Beta-glucosidase from Kluyveromyces marxianus in complex with glucoseCrystal structure of Beta-glucosidase from Kluyveromyces marxianus in complex with glucose

Structural highlights

3ac0 is a 4 chain structure with sequence from Kluyveromyces marxianus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.54Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

D1GCC6_KLUMA

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

3ac0, resolution 2.54Å

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