2bhu

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[[Image:2bhu.gif|left|200px]]<br /><applet load="2bhu" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bhu.gif|left|200px]]
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caption="2bhu, resolution 1.10&Aring;" />
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'''CRYSTAL STRUCTURE OF DEINOCOCCUS RADIODURANS MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE'''<br />
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{{Structure
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|PDB= 2bhu |SIZE=350|CAPTION= <scene name='initialview01'>2bhu</scene>, resolution 1.10&Aring;
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|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> and <scene name='pdbligand=PGE:TRIETHYLENE GLYCOL'>PGE</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF DEINOCOCCUS RADIODURANS MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2BHU 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 <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=TRS:'>TRS</scene> and <scene name='pdbligand=PGE:'>PGE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] Known structural/functional Site: <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BHU OCA].
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2BHU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BHU OCA].
==Reference==
==Reference==
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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]
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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://www.ncbi.nlm.nih.gov/pubmed/15784255 15784255]
[[Category: Alpha-amylase]]
[[Category: Alpha-amylase]]
[[Category: Deinococcus radiodurans]]
[[Category: Deinococcus radiodurans]]
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[[Category: trehalose]]
[[Category: trehalose]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:02:09 2008''

Revision as of 14:02, 20 March 2008


PDB ID 2bhu

Drag the structure with the mouse to rotate
, resolution 1.10Å
Sites:
Ligands: , and
Activity: Alpha-amylase, with EC number 3.2.1.1
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF DEINOCOCCUS RADIODURANS MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE


Overview

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

2BHU is a Single protein structure of sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA.

Reference

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

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