From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1ggg.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1ggg.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1ggg| PDB=1ggg | SCENE= }} | | {{STRUCTURE_1ggg| PDB=1ggg | SCENE= }} |
| | | | |
| - | '''GLUTAMINE BINDING PROTEIN OPEN LIGAND-FREE STRUCTURE'''
| + | ===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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_8831790}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8831790 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_8831790}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| | [[Category: Glnbp]] | | [[Category: Glnbp]] |
| | [[Category: Open form]] | | [[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 Tue Jul 1 05:14:56 2008'' |
Revision as of 02:14, 1 July 2008
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
