1uek
From Proteopedia
(New page: 200px<br /><applet load="1uek" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uek, resolution 1.70Å" /> '''Crystal structure of...) |
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| - | [[Image:1uek.jpg|left|200px]]<br /><applet load="1uek" size=" | + | [[Image:1uek.jpg|left|200px]]<br /><applet load="1uek" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1uek, resolution 1.70Å" /> | caption="1uek, resolution 1.70Å" /> | ||
'''Crystal structure of 4-(cytidine 5'-diphospho)-2C-methyl-D-erythritol kinase'''<br /> | '''Crystal structure of 4-(cytidine 5'-diphospho)-2C-methyl-D-erythritol kinase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the enzyme 4-(cytidine | + | The crystal structure of the enzyme 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol (CDP-ME) kinase from the thermophilic bacterium Thermus thermophilus HB8 has been determined at 1.7-A resolution. This enzyme catalyzes phosphorylation of the 2-hydroxyl group of CDP-ME, the fourth step of the non-mevalonate pathway, which is essential for isoprenoid biosynthesis in several pathogenic microorganisms. Since this pathway is absent in humans, it is an important target for the development of novel antimicrobial compounds. The structure of the enzyme is similar to the structures of mevalonate kinase and homoserine kinase, members of the GHMP superfamily. Lys8 and Asp125 are active site residues in mevalonate kinase that also appear to play a catalytic role in CDP-ME kinase. Both the mevalonate and the non-mevalonate pathways therefore involve closely related kinases with similar mechanisms. Assaying the enzyme showed that CDP-ME kinase will phosphorylate CDP-ME but not 4-(uridine 5'-diphospho)-2-C-methyl-D-erythritol, indicating the substrate pyrimidine moiety is involved in important interactions with the enzyme. |
==About this Structure== | ==About this Structure== | ||
| - | 1UEK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [http://en.wikipedia.org/wiki/4-(cytidine_5'-diphospho)-2-C-methyl-D-erythritol_kinase 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.148 2.7.1.148] Full crystallographic information is available from [http:// | + | 1UEK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [http://en.wikipedia.org/wiki/4-(cytidine_5'-diphospho)-2-C-methyl-D-erythritol_kinase 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.148 2.7.1.148] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UEK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
[[Category: Kuramitsu, S.]] | [[Category: Kuramitsu, S.]] | ||
| - | [[Category: Park, S | + | [[Category: Park, S Y.]] |
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
| - | [[Category: Tame, J | + | [[Category: Tame, J R.H.]] |
[[Category: Wada, T.]] | [[Category: Wada, T.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:23:40 2008'' |
Revision as of 13:23, 21 February 2008
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Crystal structure of 4-(cytidine 5'-diphospho)-2C-methyl-D-erythritol kinase
Overview
The crystal structure of the enzyme 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol (CDP-ME) kinase from the thermophilic bacterium Thermus thermophilus HB8 has been determined at 1.7-A resolution. This enzyme catalyzes phosphorylation of the 2-hydroxyl group of CDP-ME, the fourth step of the non-mevalonate pathway, which is essential for isoprenoid biosynthesis in several pathogenic microorganisms. Since this pathway is absent in humans, it is an important target for the development of novel antimicrobial compounds. The structure of the enzyme is similar to the structures of mevalonate kinase and homoserine kinase, members of the GHMP superfamily. Lys8 and Asp125 are active site residues in mevalonate kinase that also appear to play a catalytic role in CDP-ME kinase. Both the mevalonate and the non-mevalonate pathways therefore involve closely related kinases with similar mechanisms. Assaying the enzyme showed that CDP-ME kinase will phosphorylate CDP-ME but not 4-(uridine 5'-diphospho)-2-C-methyl-D-erythritol, indicating the substrate pyrimidine moiety is involved in important interactions with the enzyme.
About this Structure
1UEK is a Single protein structure of sequence from Thermus thermophilus. Active as 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase, with EC number 2.7.1.148 Full crystallographic information is available from OCA.
Reference
Crystal structure of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis., Wada T, Kuzuyama T, Satoh S, Kuramitsu S, Yokoyama S, Unzai S, Tame JR, Park SY, J Biol Chem. 2003 Aug 8;278(32):30022-7. Epub 2003 May 27. PMID:12771135
Page seeded by OCA on Thu Feb 21 15:23:40 2008
Categories: 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase | Single protein | Thermus thermophilus | Kuramitsu, S. | Park, S Y. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Tame, J R.H. | Wada, T. | Yokoyama, S. | Ghmp superfamily | Non-mevalonate pathway | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics
