1g4e: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1g4e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G4E FirstGlance]. <br>
<table><tr><td colspan='2'>[[1g4e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G4E FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2tps|2tps]], [[1g4s|1g4s]], [[1g4p|1g4p]], [[1g4t|1g4t]], [[1g6c|1g6c]], [[1g67|1g67]], [[1g69|1g69]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2tps|2tps]], [[1g4s|1g4s]], [[1g4p|1g4p]], [[1g4t|1g4t]], [[1g6c|1g6c]], [[1g67|1g67]], [[1g69|1g69]]</td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">THIC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">THIC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiamine-phosphate_diphosphorylase Thiamine-phosphate diphosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.3 2.5.1.3] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiamine-phosphate_diphosphorylase Thiamine-phosphate diphosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.3 2.5.1.3] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g4e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g4e RCSB], [http://www.ebi.ac.uk/pdbsum/1g4e PDBsum]</span></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=1g4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g4e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g4e RCSB], [http://www.ebi.ac.uk/pdbsum/1g4e PDBsum]</span></td></tr>
<table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Thiamine-phosphate diphosphorylase]]
[[Category: Thiamine-phosphate diphosphorylase]]
[[Category: Begley, T P.]]
[[Category: Begley, T P]]
[[Category: Campobasso, N.]]
[[Category: Campobasso, N]]
[[Category: Chiu, H J.]]
[[Category: Chiu, H J]]
[[Category: Ealick, S E.]]
[[Category: Ealick, S E]]
[[Category: Peapus, D H.]]
[[Category: Peapus, D H]]
[[Category: Reddick, J J.]]
[[Category: Reddick, J J]]
[[Category: Thiamin biosynthesis]]
[[Category: Thiamin biosynthesis]]
[[Category: Tim barrel]]
[[Category: Tim barrel]]
[[Category: Transferase]]
[[Category: Transferase]]

Revision as of 02:27, 23 December 2014

THIAMIN PHOSPHATE SYNTHASETHIAMIN PHOSPHATE SYNTHASE

Structural highlights

1g4e is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:THIC (Bacillus subtilis)
Activity:Thiamine-phosphate diphosphorylase, with EC number 2.5.1.3
Resources:FirstGlance, OCA, RCSB, PDBsum

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

Thiamin phosphate synthase catalyzes the formation of thiamin phosphate from 4-amino-5-(hydroxymethyl)-2-methylpyrimidine pyrophosphate and 5-(hydroxyethyl)-4-methylthiazole phosphate. Several lines of evidence suggest that the reaction proceeds via a dissociative mechanism. The previously determined crystal structure of thiamin phosphate synthase in complex with the reaction products, thiamin phosphate and magnesium pyrophosphate, provided a view of the active site and suggested a number of additional experiments. We report here seven new crystal structures primarily involving crystals of S130A thiamin phosphate synthase soaked in solutions containing substrates or products. We prepared S130A thiamin phosphate synthase with the intent of characterizing the enzyme-substrate complex. Surprisingly, in three thiamin phosphate synthase structures, the active site density cannot be modeled as either substrates or products. For these structures, the best fit to the electron density is provided by a model that consists of independent pyrimidine, pyrophosphate, and thiazole phosphate fragments, consistent with a carbenium ion intermediate. The resulting carbenium ion is likely to be further stabilized by proton transfer from the pyrimidine amino group to the pyrophosphate to give the pyrimidine iminemethide, which we believe is the species that is observed in the crystal structures.

Structural characterization of the enzyme-substrate, enzyme-intermediate, and enzyme-product complexes of thiamin phosphate synthase.,Peapus DH, Chiu HJ, Campobasso N, Reddick JJ, Begley TP, Ealick SE Biochemistry. 2001 Aug 28;40(34):10103-14. PMID:11513589[1]

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

References

  1. Peapus DH, Chiu HJ, Campobasso N, Reddick JJ, Begley TP, Ealick SE. Structural characterization of the enzyme-substrate, enzyme-intermediate, and enzyme-product complexes of thiamin phosphate synthase. Biochemistry. 2001 Aug 28;40(34):10103-14. PMID:11513589

1g4e, resolution 1.60Å

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