1ggg
From Proteopedia
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'''GLUTAMINE BINDING PROTEIN OPEN LIGAND-FREE STRUCTURE''' | '''GLUTAMINE BINDING PROTEIN OPEN LIGAND-FREE STRUCTURE''' | ||
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[[Category: Sun, Y J.]] | [[Category: Sun, Y J.]] | ||
[[Category: Wang, B C.]] | [[Category: Wang, B C.]] | ||
| - | [[Category: | + | [[Category: Amino-acid transport]] |
| - | [[Category: | + | [[Category: Binding protein]] |
| - | [[Category: | + | [[Category: Glnbp]] |
| - | [[Category: | + | [[Category: Open form]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:31:54 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:31, 2 May 2008
GLUTAMINE BINDING PROTEIN OPEN LIGAND-FREE STRUCTURE
Overview
The crystal structure of the glutamine-binding protein (GlnBP) from Escherichia coli in a ligand-free "open" conformational state has been determined by isomorphous replacement methods and refined to an R-value of 21.4% at 2.3 A resolution. There are two molecules in the asymmetric unit, related by pseudo 4-fold screw symmetry. The refined model consists of 3587 non-hydrogen atoms from 440 residues (two monomers), and 159 water molecules. The structure has root-mean-square deviations of 0.013 A from "ideal" bond lengths and 1.5 degrees from "ideal" bond angles. The GlnBP molecule has overall dimensions of approximately 60 A x 40 A x 35 A and is made up of two domains (termed large and small), which exhibit a similar supersecondary structure, linked by two antiparallel beta-strands. The small domain contains three alpha-helices and four parallel and one antiparallel beta-strands. The large domain is similar to the small domain but contains two additional alpha-helices and three more short antiparallel beta-strands. A comparison of the secondary structural motifs of GlnBP with those of other periplasmic binding proteins is discussed. A model of the "closed form" GlnBP-Gln complex has been proposed based on the crystal structures of the histidine-binding protein-His complex and "open form" GlnBP. This model has been successfully used as a search model in the crystal structure determination of the "closed form" GlnBP-Gln complex by molecular replacement methods. The model agrees remarkably well with the crystal structure of the Gln-GlnBP complex with root-mean-square deviation of 1.29 A. Our study shows that, at least in our case, it is possible to predict one conformational state of a periplasmic binding protein from another conformational state of the protein. The glutamine-binding pockets of the model and the crystal structure are compared and the modeling technique is described.
About this Structure
1GGG is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The crystal structure of glutamine-binding protein from Escherichia coli., Hsiao CD, Sun YJ, Rose J, Wang BC, J Mol Biol. 1996 Sep 20;262(2):225-42. PMID:8831790 Page seeded by OCA on Fri May 2 17:31:54 2008
