1jxh
From Proteopedia
(New page: 200px<br /><applet load="1jxh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jxh, resolution 2.3Å" /> '''4-Amino-5-hydroxymeth...) |
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| - | [[Image:1jxh.gif|left|200px]]<br /><applet load="1jxh" size=" | + | [[Image:1jxh.gif|left|200px]]<br /><applet load="1jxh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jxh, resolution 2.3Å" /> | caption="1jxh, resolution 2.3Å" /> | ||
'''4-Amino-5-hydroxymethyl-2-methylpyrimidine Phosphate Kinase from Salmonella typhimurium'''<br /> | '''4-Amino-5-hydroxymethyl-2-methylpyrimidine Phosphate Kinase from Salmonella typhimurium'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structures of Salmonella typhimurium | + | The crystal structures of Salmonella typhimurium 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate kinase (HMPP kinase) and its complex with substrate HMP have been determined. HMPP kinase catalyzes two separate ATP-dependent phosphorylation reactions and is an essential enzyme in the thiamin biosynthetic pathway. HMPP kinase is a homodimer with one active site per monomer and is structurally homologous to members of the ribokinase family. A comparison of the structure of HMPP kinase with other members of the ribokinase family suggests an evolutionary progression. Modeling studies suggest that HMPP kinase catalyzes both of its phosphorylation reactions using in-line displacement mechanisms. We propose that the active site accommodates the two separate reactions by providing two different binding modes for the phosphate group of HMP phosphate. |
==About this Structure== | ==About this Structure== | ||
| - | 1JXH 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphomethylpyrimidine_kinase Phosphomethylpyrimidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.7 2.7.4.7] Full crystallographic information is available from [http:// | + | 1JXH 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphomethylpyrimidine_kinase Phosphomethylpyrimidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.7 2.7.4.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JXH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Begley, T | + | [[Category: Begley, T P.]] |
| - | [[Category: Bennett, E | + | [[Category: Bennett, E M.]] |
[[Category: Cheng, G.]] | [[Category: Cheng, G.]] | ||
| - | [[Category: Ealick, S | + | [[Category: Ealick, S E.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: kinase]] | [[Category: kinase]] | ||
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[[Category: thid]] | [[Category: thid]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:27:47 2008'' |
Revision as of 11:27, 21 February 2008
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4-Amino-5-hydroxymethyl-2-methylpyrimidine Phosphate Kinase from Salmonella typhimurium
Overview
The crystal structures of Salmonella typhimurium 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate kinase (HMPP kinase) and its complex with substrate HMP have been determined. HMPP kinase catalyzes two separate ATP-dependent phosphorylation reactions and is an essential enzyme in the thiamin biosynthetic pathway. HMPP kinase is a homodimer with one active site per monomer and is structurally homologous to members of the ribokinase family. A comparison of the structure of HMPP kinase with other members of the ribokinase family suggests an evolutionary progression. Modeling studies suggest that HMPP kinase catalyzes both of its phosphorylation reactions using in-line displacement mechanisms. We propose that the active site accommodates the two separate reactions by providing two different binding modes for the phosphate group of HMP phosphate.
About this Structure
1JXH is a Single protein structure of sequence from Salmonella typhimurium with as ligand. Active as Phosphomethylpyrimidine kinase, with EC number 2.7.4.7 Full crystallographic information is available from OCA.
Reference
Crystal structure of 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate kinase from Salmonella typhimurium at 2.3 A resolution., Cheng G, Bennett EM, Begley TP, Ealick SE, Structure. 2002 Feb;10(2):225-35. PMID:11839308
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