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| - | [[Image:1ggg.gif|left|200px]] | |
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| - | {{Structure
| + | ==GLUTAMINE BINDING PROTEIN OPEN LIGAND-FREE STRUCTURE== |
| - | |PDB= 1ggg |SIZE=350|CAPTION= <scene name='initialview01'>1ggg</scene>, resolution 2.3Å
| + | <StructureSection load='1ggg' size='340' side='right'caption='[[1ggg]], [[Resolution|resolution]] 2.30Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND=
| + | <table><tr><td colspan='2'>[[1ggg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GGG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GGG FirstGlance]. <br> |
| - | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | |GENE=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ggg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ggg OCA], [https://pdbe.org/1ggg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ggg RCSB], [https://www.ebi.ac.uk/pdbsum/1ggg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ggg ProSAT]</span></td></tr> |
| - | |DOMAIN=
| + | </table> |
| - | |RELATEDENTRY=
| + | == Function == |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ggg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ggg OCA], [http://www.ebi.ac.uk/pdbsum/1ggg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ggg RCSB]</span>
| + | [https://www.uniprot.org/uniprot/GLNH_ECOLI GLNH_ECOLI] Involved in a glutamine-transport system GlnHPQ. |
| - | }}
| + | == Evolutionary Conservation == |
| - | | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | '''GLUTAMINE BINDING PROTEIN OPEN LIGAND-FREE STRUCTURE'''
| + | Check<jmol> |
| - | | + | <jmolCheckbox> |
| - | | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/1ggg_consurf.spt"</scriptWhenChecked> |
| - | ==Overview== | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | 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.
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | | + | </jmolCheckbox> |
| - | ==About this Structure== | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ggg ConSurf]. |
| - | 1GGG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GGG OCA].
| + | <div style="clear:both"></div> |
| - | | + | __TOC__ |
| - | ==Reference== | + | </StructureSection> |
| - | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8831790 8831790]
| + | |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Hsiao, C D.]] | + | [[Category: Hsiao C-D]] |
| - | [[Category: Rose, J.]] | + | [[Category: Rose J]] |
| - | [[Category: Sun, Y J.]] | + | [[Category: Sun Y-J]] |
| - | [[Category: Wang, B C.]] | + | [[Category: Wang B-C]] |
| - | [[Category: amino-acid transport]]
| + | |
| - | [[Category: binding protein]]
| + | |
| - | [[Category: glnbp]]
| + | |
| - | [[Category: open form]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:43:27 2008''
| + | |
