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1w77

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Revision as of 10:06, 8 January 2020

2C-methyl-D-erythritol 4-phosphate cytidylyltransferase (IspD) from Arabidopsis thaliana

Structural highlights

1w77 is a 1 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Activity:	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, with EC number 2.7.7.60
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ISPD_ARATH] Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). Is essential for chloroplast development and required for pigments and gibberellins biosynthesis.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The homodimeric 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase contributes to the nonmevalonate pathway of isoprenoid biosynthesis. The crystal structure of the catalytic domain of the recombinant enzyme derived from the plant Arabidopsis thaliana has been solved by molecular replacement and refined to 2.0 A resolution. The structure contains cytidine monophosphate bound in the active site, a ligand that has been acquired from the bacterial expression system, and this observation suggests a mechanism for feedback regulation of enzyme activity. Comparisons with bacterial enzyme structures, in particular the enzyme from Escherichia coli, indicate that whilst individual subunits overlay well, the arrangement of subunits in each functional dimer is different. That distinct quaternary structures are available, in conjunction with the observation that the protein structure contains localized areas of disorder, suggests that conformational flexibility may contribute to the function of this enzyme.

The crystal structure of a plant 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase exhibits a distinct quaternary structure compared to bacterial homologues and a possible role in feedback regulation for cytidine monophosphate.,Gabrielsen M, Kaiser J, Rohdich F, Eisenreich W, Laupitz R, Bacher A, Bond CS, Hunter WN FEBS J. 2006 Mar;273(5):1065-73. PMID:16478479^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rohdich F, Wungsintaweekul J, Eisenreich W, Richter G, Schuhr CA, Hecht S, Zenk MH, Bacher A. Biosynthesis of terpenoids: 4-diphosphocytidyl-2C-methyl-D-erythritol synthase of Arabidopsis thaliana. Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6451-6. PMID:10841550
↑ Okada K, Kawaide H, Kuzuyama T, Seto H, Curtis IS, Kamiya Y. Antisense and chemical suppression of the nonmevalonate pathway affects ent-kaurene biosynthesis in Arabidopsis. Planta. 2002 Jun;215(2):339-44. Epub 2002 Apr 12. PMID:12029484 doi:http://dx.doi.org/10.1007/s00425-002-0762-0
↑ Hsieh MH, Chang CY, Hsu SJ, Chen JJ. Chloroplast localization of methylerythritol 4-phosphate pathway enzymes and regulation of mitochondrial genes in ispD and ispE albino mutants in Arabidopsis. Plant Mol Biol. 2008 Apr;66(6):663-73. doi: 10.1007/s11103-008-9297-5. Epub 2008 , Jan 31. PMID:18236010 doi:http://dx.doi.org/10.1007/s11103-008-9297-5
↑ Gabrielsen M, Kaiser J, Rohdich F, Eisenreich W, Laupitz R, Bacher A, Bond CS, Hunter WN. The crystal structure of a plant 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase exhibits a distinct quaternary structure compared to bacterial homologues and a possible role in feedback regulation for cytidine monophosphate. FEBS J. 2006 Mar;273(5):1065-73. PMID:16478479 doi:10.1111/j.1742-4658.2006.05133.x

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1w77"

@@ Line 1: / Line 1: @@
 ==2C-methyl-D-erythritol 4-phosphate cytidylyltransferase (IspD) from Arabidopsis thaliana==
-<StructureSection load='1w77' size='340' side='right' caption='[[1w77]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='1w77' size='340' side='right'caption='[[1w77]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1w77]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W77 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W77 FirstGlance]. <br>
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[MEP cytidylyltransferase|MEP cytidylyltransferase]]
+*[[MEP cytidylyltransferase 3D structures|MEP cytidylyltransferase 3D structures]]
 == References ==
 <references/>
@@ Line 38: / Line 38: @@
 [[Category: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase]]
 [[Category: Arath]]
+[[Category: Large Structures]]
 [[Category: Bacher, A]]
 [[Category: Bond, C S]]

1w77

From Proteopedia

Revision as of 10:06, 8 January 2020

2C-methyl-D-erythritol 4-phosphate cytidylyltransferase (IspD) from Arabidopsis thaliana

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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