2eg5

From Proteopedia

(Difference between revisions)

Revision as of 12:05, 10 February 2021

The structure of xanthosine methyltransferase

Structural highlights

2eg5 is a 4 chain structure with sequence from Cofca. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2efj
Gene:	XMT1 (COFCA)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[XMT1_COFCA] Involved in the biosynthesis of caffeine. Specific for xanthosine. Cannot use xanthosine 5'-monophosphate (XMP) as substrate. Directly produces 7-methylxanthine, and therefore the methyl transfer and nucleoside cleavage may be coupled. Catalyzes the 7-N-methylation of xanthosine, but does not have 1-N- or 3-N-methylation activity.

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

Caffeine (1,3,7-trimethylxanthine) is a secondary metabolite produced by certain plant species and an important component of coffee (Coffea arabica and Coffea canephora) and tea (Camellia sinensis). Here we describe the structures of two S-adenosyl-l-methionine-dependent N-methyltransferases that mediate caffeine biosynthesis in C. canephora 'robusta', xanthosine (XR) methyltransferase (XMT), and 1,7-dimethylxanthine methyltransferase (DXMT). Both were cocrystallized with the demethylated cofactor, S-adenosyl-L-cysteine, and substrate, either xanthosine or theobromine. Our structures reveal several elements that appear critical for substrate selectivity. Serine-316 in XMT appears central to the recognition of XR. Likewise, a change from glutamine-161 in XMT to histidine-160 in DXMT is likely to have catalytic consequences. A phenylalanine-266 to isoleucine-266 change in DXMT is also likely to be crucial for the discrimination between mono and dimethyl transferases in coffee. These key residues are probably functionally important and will guide future studies with implications for the biosynthesis of caffeine and its derivatives in plants.

The structure of two N-methyltransferases from the caffeine biosynthetic pathway.,McCarthy AA, McCarthy JG Plant Physiol. 2007 Jun;144(2):879-89. Epub 2007 Apr 13. PMID:17434991^[1]

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

References

↑ McCarthy AA, McCarthy JG. The structure of two N-methyltransferases from the caffeine biosynthetic pathway. Plant Physiol. 2007 Jun;144(2):879-89. Epub 2007 Apr 13. PMID:17434991 doi:10.1104/pp.106.094854

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2eg5"

@@ Line 1: / Line 1: @@
 ==The structure of xanthosine methyltransferase==
-<StructureSection load='2eg5' size='340' side='right' caption='[[2eg5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='2eg5' size='340' side='right'caption='[[2eg5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2eg5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cofca Cofca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EG5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EG5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2eg5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cofca Cofca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EG5 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=XTS:9-[(2R,3R,4S,5R)-3,4-DIHYDROXY-5-(HYDROXYMETHYL)OXOLAN-2-YL]-3H-PURINE-2,6-DIONE'>XTS</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=XTS:9-[(2R,3R,4S,5R)-3,4-DIHYDROXY-5-(HYDROXYMETHYL)OXOLAN-2-YL]-3H-PURINE-2,6-DIONE'>XTS</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2efj|2efj]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2efj|2efj]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XMT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=49390 COFCA])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XMT1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=49390 COFCA])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2eg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eg5 OCA], [http://pdbe.org/2eg5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2eg5 RCSB], [http://www.ebi.ac.uk/pdbsum/2eg5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2eg5 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=2eg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eg5 OCA], [https://pdbe.org/2eg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eg5 RCSB], [https://www.ebi.ac.uk/pdbsum/2eg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eg5 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/XMT1_COFCA XMT1_COFCA]] Involved in the biosynthesis of caffeine. Specific for xanthosine. Cannot use xanthosine 5'-monophosphate (XMP) as substrate. Directly produces 7-methylxanthine, and therefore the methyl transfer and nucleoside cleavage may be coupled. Catalyzes the 7-N-methylation of xanthosine, but does not have 1-N- or 3-N-methylation activity.
+[[https://www.uniprot.org/uniprot/XMT1_COFCA XMT1_COFCA]] Involved in the biosynthesis of caffeine. Specific for xanthosine. Cannot use xanthosine 5'-monophosphate (XMP) as substrate. Directly produces 7-methylxanthine, and therefore the methyl transfer and nucleoside cleavage may be coupled. Catalyzes the 7-N-methylation of xanthosine, but does not have 1-N- or 3-N-methylation activity.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 35: @@
 </StructureSection>
 [[Category: Cofca]]
+[[Category: Large Structures]]
 [[Category: McCarthy, A A]]
 [[Category: McCarthy, J G]]

2eg5

From Proteopedia

Revision as of 12:05, 10 February 2021

The structure of xanthosine methyltransferase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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