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1inj

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(New page: 200px<br /><applet load="1inj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1inj, resolution 1.55&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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'''CRYSTAL STRUCTURE OF THE APO FORM OF 4-DIPHOSPHOCYTIDYL-2-C-METHYLERYTHRITOL (CDP-ME) SYNTHETASE (YGBP) INVOLVED IN MEVALONATE INDEPENDENT ISOPRENOID BIOSYNTHESIS'''<br />
'''CRYSTAL STRUCTURE OF THE APO FORM OF 4-DIPHOSPHOCYTIDYL-2-C-METHYLERYTHRITOL (CDP-ME) SYNTHETASE (YGBP) INVOLVED IN MEVALONATE INDEPENDENT ISOPRENOID BIOSYNTHESIS'''<br />
==Overview==
==Overview==
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The YgbP protein of Escherichia coli encodes the enzyme, 4-diphosphocytidyl-2-C-methylerythritol (CDP-ME) synthetase, a member of, the cytidyltransferase family of enzymes. CDP-ME is an intermediate in the, mevalonate-independent pathway for isoprenoid biosynthesis in a number of, prokaryotic organisms, algae, the plant plastids and the malaria parasite., Because vertebrates synthesize isoprenoid precursors using a mevalonate, pathway, CDP-ME synthetase and other enzymes of the mevalonate-independent, pathway for isoprenoid production represent attractive targets for the, structure-based design of selective antibacterial, herbicidal and, antimalarial drugs. The high-resolution structures of E. coli CDP-ME, synthetase in the apo form and complexed with both CTP-Mg2+ and, CDP-ME-Mg2+ reveal the stereochemical principles underlying both substrate, and product recognition as well as catalysis in CDP-ME synthetase., Moreover, these complexes represent the first experimental structures for, any cytidyltransferase with both substrates and products bound.
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The YgbP protein of Escherichia coli encodes the enzyme 4-diphosphocytidyl-2-C-methylerythritol (CDP-ME) synthetase, a member of the cytidyltransferase family of enzymes. CDP-ME is an intermediate in the mevalonate-independent pathway for isoprenoid biosynthesis in a number of prokaryotic organisms, algae, the plant plastids and the malaria parasite. Because vertebrates synthesize isoprenoid precursors using a mevalonate pathway, CDP-ME synthetase and other enzymes of the mevalonate-independent pathway for isoprenoid production represent attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs. The high-resolution structures of E. coli CDP-ME synthetase in the apo form and complexed with both CTP-Mg2+ and CDP-ME-Mg2+ reveal the stereochemical principles underlying both substrate and product recognition as well as catalysis in CDP-ME synthetase. Moreover, these complexes represent the first experimental structures for any cytidyltransferase with both substrates and products bound.
==About this Structure==
==About this Structure==
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1INJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1INJ OCA].
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1INJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1INJ OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bowman, M.E.]]
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[[Category: Bowman, M E.]]
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[[Category: Cane, D.E.]]
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[[Category: Cane, D E.]]
[[Category: Chow, C.]]
[[Category: Chow, C.]]
[[Category: Kang, I.]]
[[Category: Kang, I.]]
[[Category: Kwiatkowski, W.]]
[[Category: Kwiatkowski, W.]]
[[Category: Lillo, A.]]
[[Category: Lillo, A.]]
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[[Category: Noel, J.P.]]
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[[Category: Noel, J P.]]
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[[Category: Richard, S.B.]]
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[[Category: Richard, S B.]]
[[Category: CA]]
[[Category: CA]]
[[Category: apo form]]
[[Category: apo form]]
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[[Category: ygbp]]
[[Category: ygbp]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:31:23 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:37 2008''

Revision as of 11:13, 21 February 2008


1inj, resolution 1.55Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF THE APO FORM OF 4-DIPHOSPHOCYTIDYL-2-C-METHYLERYTHRITOL (CDP-ME) SYNTHETASE (YGBP) INVOLVED IN MEVALONATE INDEPENDENT ISOPRENOID BIOSYNTHESIS

Overview

The YgbP protein of Escherichia coli encodes the enzyme 4-diphosphocytidyl-2-C-methylerythritol (CDP-ME) synthetase, a member of the cytidyltransferase family of enzymes. CDP-ME is an intermediate in the mevalonate-independent pathway for isoprenoid biosynthesis in a number of prokaryotic organisms, algae, the plant plastids and the malaria parasite. Because vertebrates synthesize isoprenoid precursors using a mevalonate pathway, CDP-ME synthetase and other enzymes of the mevalonate-independent pathway for isoprenoid production represent attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs. The high-resolution structures of E. coli CDP-ME synthetase in the apo form and complexed with both CTP-Mg2+ and CDP-ME-Mg2+ reveal the stereochemical principles underlying both substrate and product recognition as well as catalysis in CDP-ME synthetase. Moreover, these complexes represent the first experimental structures for any cytidyltransferase with both substrates and products bound.

About this Structure

1INJ is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of 4-diphosphocytidyl-2-C- methylerythritol synthetase involved in mevalonate- independent isoprenoid biosynthesis., Richard SB, Bowman ME, Kwiatkowski W, Kang I, Chow C, Lillo AM, Cane DE, Noel JP, Nat Struct Biol. 2001 Jul;8(7):641-8. PMID:11427897

Page seeded by OCA on Thu Feb 21 13:13:37 2008

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