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1ggg

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[[Image:1ggg.gif|left|200px]]<br /><applet load="1ggg" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ggg, resolution 2.3&Aring;" />
 
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'''GLUTAMINE BINDING PROTEIN OPEN LIGAND-FREE STRUCTURE'''<br />
 
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==Overview==
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==GLUTAMINE BINDING PROTEIN OPEN LIGAND-FREE STRUCTURE==
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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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<StructureSection load='1ggg' size='340' side='right'caption='[[1ggg]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<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>
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1GGG is a [http://en.wikipedia.org/wiki/Single_protein 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].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<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>
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==Reference==
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</table>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8831790 8831790]
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== Function ==
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[https://www.uniprot.org/uniprot/GLNH_ECOLI GLNH_ECOLI] Involved in a glutamine-transport system GlnHPQ.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/1ggg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hsiao, C D.]]
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[[Category: Hsiao C-D]]
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[[Category: Rose, J.]]
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[[Category: Rose J]]
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[[Category: Sun, Y J.]]
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[[Category: Sun Y-J]]
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[[Category: Wang, B C.]]
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[[Category: Wang B-C]]
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[[Category: amino-acid transport]]
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[[Category: binding protein]]
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[[Category: glnbp]]
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[[Category: open form]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:49:47 2008''
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Current revision

GLUTAMINE BINDING PROTEIN OPEN LIGAND-FREE STRUCTURE

PDB ID 1ggg

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