1elj
From Proteopedia
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|PDB= 1elj |SIZE=350|CAPTION= <scene name='initialview01'>1elj</scene>, resolution 1.85Å | |PDB= 1elj |SIZE=350|CAPTION= <scene name='initialview01'>1elj</scene>, resolution 1.85Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1omp|1OMP]], [[3mbp|3MBP]], [[4mbp|4MBP]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1elj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elj OCA], [http://www.ebi.ac.uk/pdbsum/1elj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1elj RCSB]</span> | ||
}} | }} | ||
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[[Category: Routzahn, K M.]] | [[Category: Routzahn, K M.]] | ||
[[Category: Waugh, D S.]] | [[Category: Waugh, D S.]] | ||
| - | [[Category: SO4]] | ||
[[Category: abc transporter fold]] | [[Category: abc transporter fold]] | ||
[[Category: maltose binding protein]] | [[Category: maltose binding protein]] | ||
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[[Category: thermophilic protein]] | [[Category: thermophilic protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:05:01 2008'' |
Revision as of 17:05, 30 March 2008
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| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1OMP, 3MBP, 4MBP
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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