|
|
| Line 3: |
Line 3: |
| | <StructureSection load='3ix1' size='340' side='right'caption='[[3ix1]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='3ix1' size='340' side='right'caption='[[3ix1]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ix1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bachd Bachd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IX1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IX1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ix1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_halodurans_C-125 Alkalihalobacillus halodurans C-125]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IX1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IX1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NFM:N-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]FORMAMIDE'>NFM</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2qry|2qry]], [[3e4r|3e4r]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NFM:N-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]FORMAMIDE'>NFM</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BH2682 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272558 BACHD])</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=3ix1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ix1 OCA], [https://pdbe.org/3ix1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ix1 RCSB], [https://www.ebi.ac.uk/pdbsum/3ix1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ix1 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=3ix1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ix1 OCA], [https://pdbe.org/3ix1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ix1 RCSB], [https://www.ebi.ac.uk/pdbsum/3ix1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ix1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/THIY_BACHD THIY_BACHD]] Participates in a thiamine pyrimidine salvage pathway as part of the ABC transporter complex ThiXYZ involved in the import of thiamine degradation products. Binds the formylaminopyrimidine N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine (FAMP). Does not bind thiamine.<ref>PMID:17618314</ref> <ref>PMID:20873853</ref>
| + | [https://www.uniprot.org/uniprot/THIY_HALH5 THIY_HALH5] Participates in a thiamine pyrimidine salvage pathway as part of the ABC transporter complex ThiXYZ involved in the import of thiamine degradation products. Binds the formylaminopyrimidine N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine (FAMP). Does not bind thiamine.<ref>PMID:17618314</ref> <ref>PMID:20873853</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bachd]] | + | [[Category: Alkalihalobacillus halodurans C-125]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bale, S]] | + | [[Category: Bale S]] |
| - | [[Category: Begley, T P]] | + | [[Category: Begley TP]] |
| - | [[Category: Ealick, S E]] | + | [[Category: Ealick SE]] |
| - | [[Category: Perry, K]] | + | [[Category: Perry K]] |
| - | [[Category: Rajashankar, K R]] | + | [[Category: Rajashankar KR]] |
| - | [[Category: Biosynthetic protein]]
| + | |
| - | [[Category: Periplasmic n-formyl-4-amino-5-aminomethyl-2-methylpyrimidine binding protein]]
| + | |
| - | [[Category: Thiamine biosynthesis]]
| + | |
| Structural highlights
Function
THIY_HALH5 Participates in a thiamine pyrimidine salvage pathway as part of the ABC transporter complex ThiXYZ involved in the import of thiamine degradation products. Binds the formylaminopyrimidine N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine (FAMP). Does not bind thiamine.[1] [2]
Publication Abstract from PubMed
The ATP-binding cassette transporter system ThiXYZ transports N-formyl-4-amino-5-(aminomethyl)-2-methylpyrimidine (FAMP), a thiamin salvage pathway intermediate, into cells. FAMP is then converted to 4-amino-5-(hydroxymethyl)-2-methylpyrimidine (HMP) and recycled into the thiamin biosynthetic pathway. ThiY is the periplasmic substrate binding protein of the ThiXYZ system and delivers the substrate FAMP to the transmembrane domain. We report the crystal structure of Bacillus halodurans ThiY with FAMP bound at 2.4 A resolution determined by single-wavelength anomalous diffraction phasing. The crystal structure reveals that ThiY belongs to the group II periplasmic binding protein family. The closest structural homologues of ThiY are periplasmic binding proteins involved in alkanesulfonate/nitrate and bicarbonate transport. ThiY is also structurally homologous to thiamin binding protein (TbpA) and to thiaminase-I. THI5 is responsible for the synthesis of 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate in the thiamin biosynthetic pathway of eukaryotes and is approximately 25% identical in sequence with ThiY. A homology model of Saccharomyces cerevisiae THI5 was generated on the basis of the structure of ThiY. Many features of the thiamin pyrimidine binding site are shared between ThiY and THI5, suggesting a common ancestor.
HMP Binding Protein ThiY and HMP-P Synthase THI5 Are Structural Homologues .,Bale S, Rajashankar KR, Perry K, Begley TP, Ealick SE Biochemistry. 2010 Oct 19;49(41):8929-36. PMID:20873853[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jenkins AH, Schyns G, Potot S, Sun G, Begley TP. A new thiamin salvage pathway. Nat Chem Biol. 2007 Aug;3(8):492-7. Epub 2007 Jul 8. PMID:17618314 doi:http://dx.doi.org/10.1038/nchembio.2007.13
- ↑ Bale S, Rajashankar KR, Perry K, Begley TP, Ealick SE. HMP Binding Protein ThiY and HMP-P Synthase THI5 Are Structural Homologues . Biochemistry. 2010 Oct 19;49(41):8929-36. PMID:20873853 doi:10.1021/bi101209t
- ↑ Bale S, Rajashankar KR, Perry K, Begley TP, Ealick SE. HMP Binding Protein ThiY and HMP-P Synthase THI5 Are Structural Homologues . Biochemistry. 2010 Oct 19;49(41):8929-36. PMID:20873853 doi:10.1021/bi101209t
|
