1elj
From Proteopedia
(New page: 200px<br /><applet load="1elj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1elj, resolution 1.85Å" /> '''THE CRYSTAL STRUCTUR...) |
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| - | [[Image:1elj.gif|left|200px]]<br /><applet load="1elj" size=" | + | [[Image:1elj.gif|left|200px]]<br /><applet load="1elj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1elj, resolution 1.85Å" /> | caption="1elj, resolution 1.85Å" /> | ||
'''THE CRYSTAL STRUCTURE OF LIGANDED MALTODEXTRIN-BINDING PROTEIN FROM PYROCOCCUS FURIOSUS'''<br /> | '''THE CRYSTAL STRUCTURE OF LIGANDED MALTODEXTRIN-BINDING PROTEIN FROM PYROCOCCUS FURIOSUS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A maltodextrin-binding protein from Pyrococcus furiosus (PfuMBP) has been | + | A maltodextrin-binding protein from Pyrococcus furiosus (PfuMBP) has been overproduced in Escherichia coli, purified, and crystallized. The crystal structure of the protein bound to an oligosaccharide ligand was determined to 1.85 A resolution. The fold of PfuMBP is very similar to that of the orthologous MBP from E. coli (EcoMBP), despite the moderate level of sequence identity between the two proteins (27 % identity, 46 % similarity). PfuMBP is extremely resistant to heat and chemical denaturation, which may be attributed to a number of factors, such as a tightly packed hydrophobic core, clusters of isoleucine residues, salt-bridges, and the presence of proline residues in key positions. Surprisingly, an attempt to crystallize the complex of PfuMBP with maltose resulted in a structure that contained maltotriose in the ligand-binding site. The structure of the complex suggests that there is a considerable energy gain upon binding of maltotriose in comparison to maltose. Moreover, isothermal titration calorimetry experiments demonstrated that the binding of maltotriose to the protein is exothermic and tight, whereas no thermal effect was observed upon addition of maltose at three temperatures. Therefore, PfuMBP evidently is designed to bind oligosaccharides composed of three or more glucopyranose units. |
==About this Structure== | ==About this Structure== | ||
| - | 1ELJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1ELJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
| - | [[Category: Anderson, E | + | [[Category: Anderson, E D.]] |
| - | [[Category: Evdokimov, A | + | [[Category: Evdokimov, A G.]] |
| - | [[Category: Routzahn, K | + | [[Category: Routzahn, K M.]] |
| - | [[Category: Waugh, D | + | [[Category: Waugh, D S.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: abc transporter fold]] | [[Category: abc transporter fold]] | ||
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[[Category: thermophilic protein]] | [[Category: thermophilic protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:29:02 2008'' |
Revision as of 10:29, 21 February 2008
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THE CRYSTAL STRUCTURE OF LIGANDED MALTODEXTRIN-BINDING PROTEIN FROM PYROCOCCUS FURIOSUS
Overview
A maltodextrin-binding protein from Pyrococcus furiosus (PfuMBP) has been overproduced in Escherichia coli, purified, and crystallized. The crystal structure of the protein bound to an oligosaccharide ligand was determined to 1.85 A resolution. The fold of PfuMBP is very similar to that of the orthologous MBP from E. coli (EcoMBP), despite the moderate level of sequence identity between the two proteins (27 % identity, 46 % similarity). PfuMBP is extremely resistant to heat and chemical denaturation, which may be attributed to a number of factors, such as a tightly packed hydrophobic core, clusters of isoleucine residues, salt-bridges, and the presence of proline residues in key positions. Surprisingly, an attempt to crystallize the complex of PfuMBP with maltose resulted in a structure that contained maltotriose in the ligand-binding site. The structure of the complex suggests that there is a considerable energy gain upon binding of maltotriose in comparison to maltose. Moreover, isothermal titration calorimetry experiments demonstrated that the binding of maltotriose to the protein is exothermic and tight, whereas no thermal effect was observed upon addition of maltose at three temperatures. Therefore, PfuMBP evidently is designed to bind oligosaccharides composed of three or more glucopyranose units.
About this Structure
1ELJ is a Protein complex structure of sequences from Pyrococcus furiosus with as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis for oligosaccharide recognition by Pyrococcus furiosus maltodextrin-binding protein., Evdokimov AG, Anderson DE, Routzahn KM, Waugh DS, J Mol Biol. 2001 Jan 26;305(4):891-904. PMID:11162100
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