1us4: Difference between revisions
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[[Image:1us4. | [[Image:1us4.jpg|left|200px]]<br /><applet load="1us4" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1us4" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1us4, resolution 1.75Å" /> | caption="1us4, resolution 1.75Å" /> | ||
'''PUTATIVE GLUR0 LIGAND BINDING CORE WITH L-GLUTAMATE'''<br /> | '''PUTATIVE GLUR0 LIGAND BINDING CORE WITH L-GLUTAMATE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1US4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with GLU and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. | 1US4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with GLU and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=EGL:GLU Binding Site For Chain A'>EGL</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1US4 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:08:51 2007'' | ||
Revision as of 18:59, 18 December 2007
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PUTATIVE GLUR0 LIGAND BINDING CORE WITH L-GLUTAMATE
OverviewOverview
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.
About this StructureAbout this Structure
1US4 is a Single protein structure of sequence from Thermus thermophilus with GLU and EDO as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Structure of the Thermus thermophilus putative periplasmic glutamate/glutamine-binding protein., Takahashi H, Inagaki E, Kuroishi C, Tahirov TH, Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1846-54. Epub 2004, Sep 23. PMID:15388932
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