2yrf

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[[Image:2yrf.jpg|left|200px]]<br /><applet load="2yrf" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2yrf.jpg|left|200px]]
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caption="2yrf, resolution 2.70&Aring;" />
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'''Crystal structure of 5-methylthioribose 1-phosphate isomerase from Bacillus subtilis complexed with sulfate ion'''<br />
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{{Structure
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|PDB= 2yrf |SIZE=350|CAPTION= <scene name='initialview01'>2yrf</scene>, resolution 2.70&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/S-methyl-5-thioribose-1-phosphate_isomerase S-methyl-5-thioribose-1-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.23 5.3.1.23]
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|GENE= mtnA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
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}}
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'''Crystal structure of 5-methylthioribose 1-phosphate isomerase from Bacillus subtilis complexed with sulfate ion'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2YRF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/S-methyl-5-thioribose-1-phosphate_isomerase S-methyl-5-thioribose-1-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.23 5.3.1.23] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YRF OCA].
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2YRF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YRF OCA].
==Reference==
==Reference==
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Crystal structure of 5-methylthioribose 1-phosphate isomerase product complex from Bacillus subtilis: implications for catalytic mechanism., Tamura H, Saito Y, Ashida H, Inoue T, Kai Y, Yokota A, Matsumura H, Protein Sci. 2008 Jan;17(1):126-35. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18156470 18156470]
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Crystal structure of 5-methylthioribose 1-phosphate isomerase product complex from Bacillus subtilis: implications for catalytic mechanism., Tamura H, Saito Y, Ashida H, Inoue T, Kai Y, Yokota A, Matsumura H, Protein Sci. 2008 Jan;17(1):126-35. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18156470 18156470]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: S-methyl-5-thioribose-1-phosphate isomerase]]
[[Category: S-methyl-5-thioribose-1-phosphate isomerase]]
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[[Category: methionine salvage pathway]]
[[Category: methionine salvage pathway]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:57:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:48:36 2008''

Revision as of 16:48, 20 March 2008


PDB ID 2yrf

Drag the structure with the mouse to rotate
, resolution 2.70Å
Ligands:
Gene: mtnA (Bacillus subtilis)
Activity: S-methyl-5-thioribose-1-phosphate isomerase, with EC number 5.3.1.23
Coordinates: save as pdb, mmCIF, xml



Crystal structure of 5-methylthioribose 1-phosphate isomerase from Bacillus subtilis complexed with sulfate ion


Overview

The methionine salvage pathway (MSP) plays a crucial role in recycling a sulphahydryl derivative of the nucleoside. Recently, the genes and reactions in MSP from Bacillus subtilis have been identified, where 5-methylthioribose 1-phosphate isomerase (M1Pi) catalyzes a conversion of 5-methylthioribose 1-phosphate (MTR-1-P) to 5-methylthioribulose 1-phosphate (MTRu-1-P). Herein, we report the crystal structures of B. subtilis M1Pi (Bs-M1Pi) in complex with its product MTRu-1-P, and a sulfate at 2.4 and 2.7 A resolution, respectively. The electron density clearly shows the presence of each compound in the active site. The structural comparison with other homologous proteins explains how the substrate uptake of Bs-M1Pi may be induced by an open/closed transition of the active site. The highly conserved residues at the active site, namely, Cys160 and Asp240 are most likely to be involved in catalysis. The structural analysis sheds light on its catalytic mechanism of M1Pi.

About this Structure

2YRF is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Crystal structure of 5-methylthioribose 1-phosphate isomerase product complex from Bacillus subtilis: implications for catalytic mechanism., Tamura H, Saito Y, Ashida H, Inoue T, Kai Y, Yokota A, Matsumura H, Protein Sci. 2008 Jan;17(1):126-35. PMID:18156470

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