1us4
From Proteopedia
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==Overview== | ==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 ... | + | 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 Structure== | ==About this Structure== | ||
| - | 1US4 is a | + | 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]. Structure known Active Site: EGL. 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 Mon Nov 5 15:05:21 2007'' |
Revision as of 13:00, 5 November 2007
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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.
About this Structure
1US4 is a Single protein structure of sequence from Thermus thermophilus with GLU and EDO as ligands. Structure known Active Site: EGL. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 5 15:05:21 2007
Categories: Single protein | Thermus thermophilus | Inagaki, E. | RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative. | Tahirov, T.H. | Takahashi, H. | EDO | GLU | Glur0 | Glutamate receptor | L-glutamate | Membrane protein | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics
