1us4: Difference between revisions

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[[Image:1us4.~~jpg~~|left|200px]]

[[Image:1us4.png|left|200px]]

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~~'''~~PUTATIVE GLUR0 LIGAND BINDING CORE WITH L-GLUTAMATE~~'''~~

===PUTATIVE GLUR0 LIGAND BINDING CORE WITH L-GLUTAMATE===

~~==Overview==~~

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~~As part of a structural genomics project, the crystal structure of a 314~~-~~amino~~-~~acid protein encoded by Thermus thermophilus HB8 gene TT1099 was solved to 1.75 A using the multiple-wavelength anomalous dispersion (MAD) method and a selenomethionine-incorporated protein.~~ The ~~native protein structure was solved to 1.5 A using the molecular-replacement method. Both structures revealed a bound ligand~~, ~~L-glutamate or L-glutamine~~, ~~and a fold related~~ to the ~~periplasmic substrate-binding proteins~~ (~~PSBP)~~. ~~Further comparative structural analysis with other PSBP-fold proteins revealed the conservation of the predicted membrane permease binding surface area and indicated that the T~~. ~~thermophilus HB8 molecule is most likely to be an L-glutamate and/or an L-glutamine-binding protein related to the cluster 3 periplasmic receptors. However~~, ~~the geometry of ligand binding~~ is ~~unique to~~ the ~~T. thermophilus HB8 molecule~~.

The line below this paragraph, {{ABSTRACT_PUBMED_15388932}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15388932 is the PubMed ID number.

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==About this Structure==

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[[Category: Rsgi]]

[[Category: Structural genomic]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 11~~:36:53 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:13:01 2008''

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-[[Image:1us4.jpg|left|200px]]
+{{Seed}}
+[[Image:1us4.png|left|200px]]
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 {{STRUCTURE_1us4|  PDB=1us4  |  SCENE=  }}
-'''PUTATIVE GLUR0 LIGAND BINDING CORE WITH L-GLUTAMATE'''
+===PUTATIVE GLUR0 LIGAND BINDING CORE WITH L-GLUTAMATE===
-==Overview==
+<!--
-As part of a structural genomics project, the crystal structure of a 314-amino-acid protein encoded by Thermus thermophilus HB8 gene TT1099 was solved to 1.75 A using the multiple-wavelength anomalous dispersion (MAD) method and a selenomethionine-incorporated protein. The native protein structure was solved to 1.5 A using the molecular-replacement method. Both structures revealed a bound ligand, L-glutamate or L-glutamine, and a fold related to the periplasmic substrate-binding proteins (PSBP). Further comparative structural analysis with other PSBP-fold proteins revealed the conservation of the predicted membrane permease binding surface area and indicated that the T. thermophilus HB8 molecule is most likely to be an L-glutamate and/or an L-glutamine-binding protein related to the cluster 3 periplasmic receptors. However, the geometry of ligand binding is unique to the T. thermophilus HB8 molecule.
+The line below this paragraph, {{ABSTRACT_PUBMED_15388932}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15388932 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15388932}}
 ==About this Structure==
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 [[Category: Rsgi]]
 [[Category: Structural genomic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:36:53 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:13:01 2008''