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1ggg

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[[Image:1ggg.gif|left|200px]]
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{{STRUCTURE_1ggg| PDB=1ggg | SCENE= }}
{{STRUCTURE_1ggg| PDB=1ggg | SCENE= }}
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'''GLUTAMINE BINDING PROTEIN OPEN LIGAND-FREE STRUCTURE'''
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===GLUTAMINE BINDING PROTEIN OPEN LIGAND-FREE STRUCTURE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8831790 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8831790}}
==About this Structure==
==About this Structure==
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[[Category: Glnbp]]
[[Category: Glnbp]]
[[Category: Open form]]
[[Category: Open form]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:31:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:14:56 2008''

Revision as of 02:14, 1 July 2008

Image:1ggg.png

Template:STRUCTURE 1ggg

GLUTAMINE BINDING PROTEIN OPEN LIGAND-FREE STRUCTURE

Template:ABSTRACT PUBMED 8831790

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 Tue Jul 1 05:14:56 2008

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