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New page: left|200px<br /> <applet load="2bhz" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bhz, resolution 1.20Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:2bhz.gif|left|200px]]<br />
<applet load="2bhz" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2bhz, resolution 1.20&Aring;" />
'''CRYSTAL STRUCTURE OF DEINOCOCCUS RADIODURANS MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE IN COMPLEX WITH MALTOSE'''<br />


==Overview==
==Crystal structure of Deinococcus radiodurans maltooligosyltrehalose trehalohydrolase in complex with maltose==
Trehalose (alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranose) is a, non-reducing diglucoside found in various organisms that serves as a, carbohydrate reserve and as an agent that protects against a variety of, physical and chemical stresses. Deinococcus radiodurans possesses an, alternative biosynthesis pathway for the synthesis of trehalose from, maltooligosaccharides. This reaction is mediated by two enzymes:, maltooligosyltrehalose synthase (MTSase) and maltooligosyltrehalose, trehalohydrolase (MTHase). Here, we present the 1.1A resolution crystal, structure of MTHase. It consists of three major domains: two beta-sheet, domains and a conserved glycosidase (beta/alpha)8 barrel catalytic domain., Three subdomains consisting of short insertions were identified within the, catalytic ... [[http://ispc.weizmann.ac.il/pmbin/getpm?15784255 (full description)]]
<StructureSection load='2bhz' size='340' side='right'caption='[[2bhz]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bhz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BHZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BHZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=2bhz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhz OCA], [https://pdbe.org/2bhz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bhz RCSB], [https://www.ebi.ac.uk/pdbsum/2bhz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bhz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TREZ_DEIRA TREZ_DEIRA]
== 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/bh/2bhz_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2bhz ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Trehalose (alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranose) is a non-reducing diglucoside found in various organisms that serves as a carbohydrate reserve and as an agent that protects against a variety of physical and chemical stresses. Deinococcus radiodurans possesses an alternative biosynthesis pathway for the synthesis of trehalose from maltooligosaccharides. This reaction is mediated by two enzymes: maltooligosyltrehalose synthase (MTSase) and maltooligosyltrehalose trehalohydrolase (MTHase). Here, we present the 1.1A resolution crystal structure of MTHase. It consists of three major domains: two beta-sheet domains and a conserved glycosidase (beta/alpha)8 barrel catalytic domain. Three subdomains consisting of short insertions were identified within the catalytic domain. Subsequently, structures of MTHase in complex with maltose and trehalose were obtained at 1.2 A and 1.5 A resolution, respectively. These structures reveal the importance of the three inserted subdomains in providing the key residues required for substrate recognition. Trehalose is recognised specifically in the +1 and +2 binding subsites by an extensive hydrogen-bonding network and a strong hydrophobic stacking interaction in between two aromatic residues. Moreover, upon binding to maltose, which mimics the substrate sugar chain, a major concerted conformational change traps the sugar chain in the active site. The presence of magnesium in the active site of the MTHase-maltose complex suggests that MTHase activity may be regulated by divalent cations.


==About this Structure==
Crystal structure of maltooligosyltrehalose trehalohydrolase from Deinococcus radiodurans in complex with disaccharides.,Timmins J, Leiros HK, Leonard G, Leiros I, McSweeney S J Mol Biol. 2005 Apr 15;347(5):949-63. PMID:15784255<ref>PMID:15784255</ref>
2BHZ is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]] with MAL, MG, BME and TRS as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BHZ OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of maltooligosyltrehalose trehalohydrolase from Deinococcus radiodurans in complex with disaccharides., Timmins J, Leiros HK, Leonard G, Leiros I, McSweeney S, J Mol Biol. 2005 Apr 15;347(5):949-63. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15784255 15784255]
</div>
[[Category: Deinococcus radiodurans]]
<div class="pdbe-citations 2bhz" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
[[Category: Leiros, H.K.S.]]
<references/>
[[Category: Leiros, I.]]
__TOC__
[[Category: Leonard, G.]]
</StructureSection>
[[Category: Mcsweeney, S.]]
[[Category: Deinococcus radiodurans R1]]
[[Category: Timmins, J.]]
[[Category: Large Structures]]
[[Category: BME]]
[[Category: Leiros H-KS]]
[[Category: MAL]]
[[Category: Leiros I]]
[[Category: MG]]
[[Category: Leonard G]]
[[Category: TRS]]
[[Category: McSweeney S]]
[[Category: alpha-amylase]]
[[Category: Timmins J]]
[[Category: d. radiodurans]]
[[Category: desiccation resistance glycosidase]]
[[Category: hydrolase]]
[[Category: protein-carbohydrate complex]]
[[Category: trehalose]]
 
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