3abz

From Proteopedia

(Difference between revisions)

Revision as of 08:30, 4 August 2016

Crystal structure of Se-Met labeled Beta-glucosidase from Kluyveromyces marxianus

Structural highlights

3abz is a 4 chain structure with sequence from Cbs 712. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	3ac0
Gene:	Bgl, bglI (CBS 712)
Activity:	Beta-glucosidase, with EC number 3.2.1.21
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

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

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Yoshida E, Hidaka M, Fushinobu S, Koyanagi T, Minami H, Tamaki H, Kitaoka M, Katayama T, Kumagai H. Role of a PA14 domain in determining substrate specificity of a glycoside hydrolase family 3 beta-glucosidase from Kluyveromyces marxianus. Biochem J. 2010 Jul 27. PMID:20662765 doi:10.1042/BJ20100351

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3abz"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Se-Met labeled Beta-glucosidase from Kluyveromyces marxianus==
 <StructureSection load='3abz' size='340' side='right' caption='[[3abz]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3abz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Kluyveromyces_marxianus Kluyveromyces marxianus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ABZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ABZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3abz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_712 Cbs 712]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ABZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ABZ FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ac0|3ac0]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Bgl, bglI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4911 Kluyveromyces marxianus])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Bgl, bglI ([http://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'>[http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3abz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3abz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3abz RCSB], [http://www.ebi.ac.uk/pdbsum/3abz PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3abz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3abz OCA], [http://pdbe.org/3abz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3abz RCSB], [http://www.ebi.ac.uk/pdbsum/3abz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3abz ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 18: / Line 19: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata 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=3abz ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3abz" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 36: / Line 38: @@
 </StructureSection>
 [[Category: Beta-glucosidase]]
-[[Category: Kluyveromyces marxianus]]
+[[Category: Cbs 712]]
 [[Category: Fushinobu, S]]
 [[Category: Hidaka, M]]

3abz

From Proteopedia

Revision as of 08:30, 4 August 2016

Crystal structure of Se-Met labeled Beta-glucosidase from Kluyveromyces marxianus

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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