1bc5

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[[Image:1bc5.gif|left|200px]]<br /><applet load="1bc5" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1bc5.gif|left|200px]]<br /><applet load="1bc5" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1bc5, resolution 2.2&Aring;" />
caption="1bc5, resolution 2.2&Aring;" />
'''CHEMOTAXIS RECEPTOR RECOGNITION BY PROTEIN METHYLTRANSFERASE CHER'''<br />
'''CHEMOTAXIS RECEPTOR RECOGNITION BY PROTEIN METHYLTRANSFERASE CHER'''<br />
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==About this Structure==
==About this Structure==
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1BC5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with CO, ACE and SAH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protein-glutamate_O-methyltransferase Protein-glutamate O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.80 2.1.1.80] Known structural/functional Site: <scene name='pdbsite=COB:Co Binding Site Is Formed By HIS 192 And HIS 114 Of Symm ...'>COB</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BC5 OCA].
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1BC5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=CO:'>CO</scene>, <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=SAH:'>SAH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protein-glutamate_O-methyltransferase Protein-glutamate O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.80 2.1.1.80] Known structural/functional Site: <scene name='pdbsite=COB:Co+Binding+Site+Is+Formed+By+HIS+192+And+HIS+114+Of+Symm+...'>COB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BC5 OCA].
==Reference==
==Reference==
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[[Category: peptide binding]]
[[Category: peptide binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:25:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:32:34 2008''

Revision as of 07:32, 3 February 2008


1bc5, resolution 2.2Å

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CHEMOTAXIS RECEPTOR RECOGNITION BY PROTEIN METHYLTRANSFERASE CHER

Overview

Signal transduction processes commonly involve reversible covalent, modifications of receptors. Bacterial chemotaxis receptors are reversibly, methylated at specific glutamate residues within coiled-coil regions of, their cytoplasmic domains. Methylation is catalyzed by an, S-adenosylmethionine-dependent protein methyltransferase, CheR, that binds, to a specific sequence at the C-termini of some chemotaxis receptors. From, this tethering point, CheR methylates neighboring receptor molecules. We, report the crystal structure, determined to 2.2 A resolution, of a complex, of the Salmonella typhimurium methyltransferase CheR bound to the, methylation reaction product, S-adenosylhomocysteine (AdoHcy), and the, C-terminal pentapeptide of the aspartate receptor, Tar. The structure, indicates the basis for the specificity of interaction between the, chemoreceptors and CheR and identifies a specific receptor binding motif, incorporated in the CheR methyltransferase domain.

About this Structure

1BC5 is a Single protein structure of sequence from Salmonella typhimurium with , and as ligands. Active as Protein-glutamate O-methyltransferase, with EC number 2.1.1.80 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Chemotaxis receptor recognition by protein methyltransferase CheR., Djordjevic S, Stock AM, Nat Struct Biol. 1998 Jun;5(6):446-50. PMID:9628482

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