3abz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "3abz" [edit=sysop:move=sysop])
Current revision (16:22, 22 December 2021) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3abz.png|left|200px]]
 
-
<!--
+
==Crystal structure of Se-Met labeled Beta-glucosidase from Kluyveromyces marxianus==
-
The line below this paragraph, containing "STRUCTURE_3abz", creates the "Structure Box" on the page.
+
<StructureSection load='3abz' size='340' side='right'caption='[[3abz]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[3abz]] 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=3ABZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ABZ FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
-
{{STRUCTURE_3abz| PDB=3abz | SCENE= }}
+
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ac0|3ac0]]</div></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=3abz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3abz OCA], [https://pdbe.org/3abz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3abz RCSB], [https://www.ebi.ac.uk/pdbsum/3abz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3abz ProSAT]</span></td></tr>
 +
</table>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ab/3abz_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<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/main_output.php?pdb_ID=3abz ConSurf].
 +
<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.
-
===Crystal structure of Se-Met labeled Beta-glucosidase from Kluyveromyces marxianus===
+
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 3abz" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_20662765}}, adds the Publication Abstract to the page
+
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 20662765 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_20662765}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
[[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].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:20662765</ref><ref group="xtra">PMID:19923748</ref><references group="xtra"/>
+
[[Category: Beta-glucosidase]]
[[Category: Beta-glucosidase]]
-
[[Category: Kluyveromyces marxianus]]
+
[[Category: Cbs 712]]
-
[[Category: Fushinobu, S.]]
+
[[Category: Large Structures]]
-
[[Category: Hidaka, M.]]
+
[[Category: Fushinobu, S]]
-
[[Category: Katayama, T.]]
+
[[Category: Hidaka, M]]
-
[[Category: Kumagai, H.]]
+
[[Category: Katayama, T]]
-
[[Category: Yoshida, E.]]
+
[[Category: Kumagai, H]]
 +
[[Category: Yoshida, E]]
[[Category: Glycoside hydrolase family3 beta-glucosidase]]
[[Category: Glycoside hydrolase family3 beta-glucosidase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Pa14 domain]]
[[Category: Pa14 domain]]

Current revision

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

PDB ID 3abz

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools