This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2xme

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 10:55, 13 April 2022

The X-ray structure of CTP:inositol-1-phosphate cytidylyltransferase from Archaeoglobus fulgidus

Structural highlights

2xme is a 12 chain structure with sequence from Arcfl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2xmh
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DIPPS_ARCFU] Involved in biosynthesis of di-myo-inositol phosphate (DIP), a widespread organic solute in microorganisms adapted to hot environments. Catalyzes the condensation of CTP and L-myo-inositol-1-phosphate into CDP-L-myo-inositol, as well as the biosynthesis of di-myo-inositol-1,3'-phosphate-1'-phosphate (DIPP) from CDP-L-myo-inositol and L-myo-inositol-1-phosphate. The cytidylyltransferase is absolutely specific for CTP and L-myo-inositol-1-P. The DIPP synthase uses only L-myoinositol-1-phosphate as an alcohol acceptor, but CDP-glycerol, as well as CDP-L-myo-inositol and CDP-D-myoinositol, are recognized as alcohol donors.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Many Archaea and Bacteria isolated from hot, marine environments accumulate di-myo-inositol-phosphate (DIP), primarily in response to heat stress. The biosynthesis of this compatible solute involves the activation of inositol to CDP-inositol via the action of a recently discovered CTP:inositol-1-phosphate cytidylyltransferase (IPCT) activity. In most cases, IPCT is part of a bifunctional enzyme comprising two domains: a cytoplasmic domain with IPCT activity and a membrane domain catalyzing the synthesis of di-myo-inositol-1,3'-phosphate-1'-phosphate from CDP-inositol and l-myo-inositol phosphate. Herein, we describe the first X-ray structure of the IPCT domain of the bifunctional enzyme from the hyperthermophilic archaeon Archaeoglobus fulgidus DSMZ 7324. The structure of the enzyme in the apo form was solved to a 1.9-A resolution. The enzyme exhibited apparent K(m) values of 0.9 and 0.6 mM for inositol-1-phosphate and CTP, respectively. The optimal temperature for catalysis was in the range 90 to 95 degrees C, and the V(max) determined at 90 degrees C was 62.9 mumol . min(-1) . mg of protein(-1). The structure of IPCT is composed of a central seven-stranded mixed beta-sheet, of which six beta-strands are parallel, surrounded by six alpha-helices, a fold reminiscent of the dinucleotide-binding Rossmann fold. The enzyme shares structural homology with other pyrophosphorylases showing the canonical motif G-X-G-T-(R/S)-X(4)-P-K. CTP, l-myo-inositol-1-phosphate, and CDP-inositol were docked into the catalytic site, which provided insights into the binding mode and high specificity of the enzyme for CTP. This work is an important step toward the final goal of understanding the full catalytic route for DIP synthesis in the native, bifunctional enzyme.

Crystal Structure of Archaeoglobus fulgidus CTP:Inositol-1-Phosphate Cytidylyltransferase, a Key Enzyme for Di-myo-Inositol-Phosphate Synthesis in (Hyper)Thermophiles.,Brito JA, Borges N, Vonrhein C, Santos H, Archer M J Bacteriol. 2011 May;193(9):2177-85. Epub 2011 Mar 4. PMID:21378188^[4]

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

References

↑ Borges N, Goncalves LG, Rodrigues MV, Siopa F, Ventura R, Maycock C, Lamosa P, Santos H. Biosynthetic pathways of inositol and glycerol phosphodiesters used by the hyperthermophile Archaeoglobus fulgidus in stress adaptation. J Bacteriol. 2006 Dec;188(23):8128-35. Epub 2006 Oct 6. PMID:17028285 doi:http://dx.doi.org/10.1128/JB.01129-06
↑ Rodrigues MV, Borges N, Henriques M, Lamosa P, Ventura R, Fernandes C, Empadinhas N, Maycock C, da Costa MS, Santos H. Bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase, the key enzyme for di-myo-inositol-phosphate synthesis in several (hyper)thermophiles. J Bacteriol. 2007 Aug;189(15):5405-12. Epub 2007 May 25. PMID:17526717 doi:http://dx.doi.org/JB.00465-07
↑ Brito JA, Borges N, Vonrhein C, Santos H, Archer M. Crystal Structure of Archaeoglobus fulgidus CTP:Inositol-1-Phosphate Cytidylyltransferase, a Key Enzyme for Di-myo-Inositol-Phosphate Synthesis in (Hyper)Thermophiles. J Bacteriol. 2011 May;193(9):2177-85. Epub 2011 Mar 4. PMID:21378188 doi:10.1128/JB.01543-10
↑ Brito JA, Borges N, Vonrhein C, Santos H, Archer M. Crystal Structure of Archaeoglobus fulgidus CTP:Inositol-1-Phosphate Cytidylyltransferase, a Key Enzyme for Di-myo-Inositol-Phosphate Synthesis in (Hyper)Thermophiles. J Bacteriol. 2011 May;193(9):2177-85. Epub 2011 Mar 4. PMID:21378188 doi:10.1128/JB.01543-10

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2xme"

@@ Line 3: / Line 3: @@
 <StructureSection load='2xme' size='340' side='right'caption='[[2xme]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2xme]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XME OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XME FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2xme]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XME FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xmh|2xmh]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xmh|2xmh]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2xme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xme OCA], [http://pdbe.org/2xme PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xme RCSB], [http://www.ebi.ac.uk/pdbsum/2xme PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xme ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xme OCA], [https://pdbe.org/2xme PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xme RCSB], [https://www.ebi.ac.uk/pdbsum/2xme PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xme ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DIPPS_ARCFU DIPPS_ARCFU]] Involved in biosynthesis of di-myo-inositol phosphate (DIP), a widespread organic solute in microorganisms adapted to hot environments. Catalyzes the condensation of CTP and L-myo-inositol-1-phosphate into CDP-L-myo-inositol, as well as the biosynthesis of di-myo-inositol-1,3'-phosphate-1'-phosphate (DIPP) from CDP-L-myo-inositol and L-myo-inositol-1-phosphate. The cytidylyltransferase is absolutely specific for CTP and L-myo-inositol-1-P. The DIPP synthase uses only L-myoinositol-1-phosphate as an alcohol acceptor, but CDP-glycerol, as well as CDP-L-myo-inositol and CDP-D-myoinositol, are recognized as alcohol donors.<ref>PMID:17028285</ref> <ref>PMID:17526717</ref> <ref>PMID:21378188</ref>
+[[https://www.uniprot.org/uniprot/DIPPS_ARCFU DIPPS_ARCFU]] Involved in biosynthesis of di-myo-inositol phosphate (DIP), a widespread organic solute in microorganisms adapted to hot environments. Catalyzes the condensation of CTP and L-myo-inositol-1-phosphate into CDP-L-myo-inositol, as well as the biosynthesis of di-myo-inositol-1,3'-phosphate-1'-phosphate (DIPP) from CDP-L-myo-inositol and L-myo-inositol-1-phosphate. The cytidylyltransferase is absolutely specific for CTP and L-myo-inositol-1-P. The DIPP synthase uses only L-myoinositol-1-phosphate as an alcohol acceptor, but CDP-glycerol, as well as CDP-L-myo-inositol and CDP-D-myoinositol, are recognized as alcohol donors.<ref>PMID:17028285</ref> <ref>PMID:17526717</ref> <ref>PMID:21378188</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2xme

From Proteopedia

Revision as of 10:55, 13 April 2022

The X-ray structure of CTP:inositol-1-phosphate cytidylyltransferase from Archaeoglobus fulgidus

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox