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1ggg

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Revision as of 06:50, 3 January 2018

GLUTAMINE BINDING PROTEIN OPEN LIGAND-FREE STRUCTURE

Structural highlights

1ggg is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GLNH_ECOLI] Involved in a glutamine-transport system GlnHPQ.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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 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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hsiao CD, Sun YJ, Rose J, Wang BC. The crystal structure of glutamine-binding protein from Escherichia coli. J Mol Biol. 1996 Sep 20;262(2):225-42. PMID:8831790 doi:10.1006/jmbi.1996.0509

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ggg"

@@ Line 1: / Line 1: @@
 ==GLUTAMINE BINDING PROTEIN OPEN LIGAND-FREE STRUCTURE==
 <StructureSection load='1ggg' size='340' side='right' caption='[[1ggg]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1ggg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GGG FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1ggg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ggg RCSB], [http://www.ebi.ac.uk/pdbsum/1ggg PDBsum]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1ggg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ggg RCSB], [http://www.ebi.ac.uk/pdbsum/1ggg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ggg ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 11: / Line 12: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/1ggg_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/1ggg_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1ggg

From Proteopedia

Revision as of 06:50, 3 January 2018

GLUTAMINE BINDING PROTEIN OPEN LIGAND-FREE STRUCTURE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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