1ggg

<table><tr><td colspan='2'>[[1ggg]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/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'>[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>

[[https://www.uniprot.org/uniprot/GLNH_ECOLI GLNH_ECOLI]] Involved in a glutamine-transport system GlnHPQ.

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== 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<ref>PMID:8831790</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Hsiao, C D]]

[[Category: Rose, J]]

[[Category: Sun, Y J]]

[[Category: Wang, B C]]

[[Category: Open form]]