2bhz
From Proteopedia
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| - | [[Image:2bhz.gif|left|200px]] | + | [[Image:2bhz.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF DEINOCOCCUS RADIODURANS MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE IN COMPLEX WITH MALTOSE''' | + | {{Structure |
| + | |PDB= 2bhz |SIZE=350|CAPTION= <scene name='initialview01'>2bhz</scene>, resolution 1.20Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene> and <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF DEINOCOCCUS RADIODURANS MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE IN COMPLEX WITH MALTOSE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BHZ is a [ | + | 2BHZ 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=2BHZ OCA]. |
==Reference== | ==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:[http:// | + | 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: TRS]] | [[Category: TRS]] | ||
[[Category: alpha-amylase]] | [[Category: alpha-amylase]] | ||
| - | [[Category: d. | + | [[Category: d. radioduran]] |
[[Category: desiccation resistance glycosidase]] | [[Category: desiccation resistance glycosidase]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: trehalose]] | [[Category: trehalose]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:02:11 2008'' |
Revision as of 14:02, 20 March 2008
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| , resolution 1.20Å | |||||||
|---|---|---|---|---|---|---|---|
| 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 IN COMPLEX WITH MALTOSE
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
2BHZ 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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