1i52: Difference between revisions

Revision as of 14:08, 21 February 2008

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

OverviewOverview

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 StructureAbout this Structure

1I52 is a Single protein structure of sequence from Escherichia coli with , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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 13:08:03 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1i52.gif|left|200px]]<br /><applet load="1i52" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1i52.gif|left|200px]]<br /><applet load="1i52" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1i52, resolution 1.50&Aring;" />
 '''CRYSTAL STRUCTURE OF 4-DIPHOSPHOCYTIDYL-2-C-METHYLERYTHRITOL (CDP-ME) SYNTHASE (YGBP) INVOLVED IN MEVALONATE INDEPENDENT ISOPRENOID BIOSYNTHESIS'''<br />
 ==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.
+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==
-I52 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, MG and CTP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I52 OCA].
+I52 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>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=CTP:'>CTP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I52 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Bowman, M.E.]]
+[[Category: Bowman, M E.]]
-[[Category: Cane, D.E.]]
+[[Category: Cane, D E.]]
 [[Category: Chow, C.]]
 [[Category: Kang, I.]]
 [[Category: Kwiatkowski, W.]]
 [[Category: Lillo, M.]]
-[[Category: Noel, J.P.]]
+[[Category: Noel, J P.]]
-[[Category: Richard, S.B.]]
+[[Category: Richard, S B.]]
 [[Category: CA]]
 [[Category: CTP]]
@@ Line 29: / Line 29: @@
 [[Category: mep]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:03:33 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:03 2008''