2bd0: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
Line 3: Line 3:
<StructureSection load='2bd0' size='340' side='right'caption='[[2bd0]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='2bd0' size='340' side='right'caption='[[2bd0]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2bd0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlte Chlte]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BD0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2bd0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlorobaculum_tepidum_TLS Chlorobaculum tepidum TLS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BD0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BIO:BIOPTERIN'>BIO</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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]] 1.7&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Sepiapterin_reductase_(L-erythro-7,8-dihydrobiopterin_forming) Sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.153 1.1.1.153] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BIO:BIOPTERIN'>BIO</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></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=2bd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bd0 OCA], [https://pdbe.org/2bd0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bd0 RCSB], [https://www.ebi.ac.uk/pdbsum/2bd0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bd0 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=2bd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bd0 OCA], [https://pdbe.org/2bd0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bd0 RCSB], [https://www.ebi.ac.uk/pdbsum/2bd0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bd0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SPRE_CHLTE SPRE_CHLTE]] Catalyzes the final reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin.<ref>PMID:10333495</ref> <ref>PMID:15621425</ref> <ref>PMID:18542834</ref>
[https://www.uniprot.org/uniprot/SPRE_CHLTE SPRE_CHLTE] Catalyzes the final reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin.<ref>PMID:10333495</ref> <ref>PMID:15621425</ref> <ref>PMID:18542834</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 20: Line 20:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bd0 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bd0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sepiapterin reductase (SR) is involved in the last step of tetrahydrobiopterin (BH(4)) biosynthesis by reducing the di-keto group of 6-pyruvoyl tetrahydropterin. Chlorobium tepidum SR (cSR) generates a distinct BH(4) product, L-threo-BH(4) (6R-(1'S,2'S)-5,6,7,8-BH(4)), whereas animal enzymes produce L-erythro-BH(4) (6R-(1'R,2'S)-5,6,7,8-BH(4)) although it has high amino acid sequence similarities to the other animal enzymes. To elucidate the structural basis for the different reaction stereospecificities, we have determined the three-dimensional structures of cSR alone and complexed with NADP and sepiapterin at 2.1 and 1.7 A resolution, respectively. The overall folding of the cSR, the binding site for the cofactor NADP(H), and the positions of active site residues were quite similar to the mouse and the human SR. However, significant differences were found in the substrate binding region of the cSR. In comparison to the mouse SR complex, the sepiapterin in the cSR is rotated about 180 degrees around the active site and bound between two aromatic side chains of Trp-196 and Phe-99 so that its pterin ring is shifted to the opposite side, but its side chain position is not changed. The swiveled sepiapterin binding results in the conversion of the side chain configuration, exposing the opposite face for hydride transfer from NADPH. The different sepiapterin binding mode within the conserved catalytic architecture presents a novel strategy of switching the reaction stereospecificities in the same protein fold.
Structure of Chlorobium tepidum sepiapterin reductase complex reveals the novel substrate binding mode for stereospecific production of L-threo-tetrahydrobiopterin.,Supangat S, Seo KH, Choi YK, Park YS, Son D, Han CD, Lee KH J Biol Chem. 2006 Jan 27;281(4):2249-56. Epub 2005 Nov 24. PMID:16308317<ref>PMID:16308317</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2bd0" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Chlte]]
[[Category: Chlorobaculum tepidum TLS]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Choi, Y K]]
[[Category: Choi YK]]
[[Category: Lee, K H]]
[[Category: Lee KH]]
[[Category: Park, Y S]]
[[Category: Park YS]]
[[Category: Seo, K H]]
[[Category: Seo KH]]
[[Category: Supangat, S]]
[[Category: Supangat S]]
[[Category: Chlorobium tepidum]]
[[Category: Oxidoreductase]]
[[Category: Sepiapterin reductase]]
Retrieved from "https://proteopedia.org/2bd0"