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1us4

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{{STRUCTURE_1us4| PDB=1us4 | SCENE= }}
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'''PUTATIVE GLUR0 LIGAND BINDING CORE WITH L-GLUTAMATE'''
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===PUTATIVE GLUR0 LIGAND BINDING CORE WITH L-GLUTAMATE===
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==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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15388932 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15388932}}
==About this Structure==
==About this Structure==
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[[Category: Rsgi]]
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[[Category: Structural genomic]]
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Revision as of 09:13, 29 July 2008

Image:1us4.png

Template:STRUCTURE 1us4

PUTATIVE GLUR0 LIGAND BINDING CORE WITH L-GLUTAMATE

Template:ABSTRACT PUBMED 15388932

About this Structure

1US4 is a Single protein structure of sequence from Thermus thermophilus. 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 Tue Jul 29 12:13:01 2008

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