3o06
From Proteopedia
(Difference between revisions)
| (7 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of yeast pyridoxal 5-phosphate synthase Snz1== | |
| + | <StructureSection load='3o06' size='340' side='right'caption='[[3o06]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3o06]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O06 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O06 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35Å</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=3o06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o06 OCA], [https://pdbe.org/3o06 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o06 RCSB], [https://www.ebi.ac.uk/pdbsum/3o06 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o06 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SNZ1_YEAST SNZ1_YEAST] Required for the production of pyridoxine (vitamin B6). May be involved in growth arrest and cellular response to nutrient limitation. Required for growth in the presence of low level of intracellular pyridoxine.<ref>PMID:12271461</ref> <ref>PMID:12649274</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In most eubacteria, fungi, apicomplexa, plants, and some metazoans, the active form of vitamin B6, pyridoxal 5-phosphate (PLP) is de novo synthesized from three substrates, ribose 5-phosphate (R5P), dihydroxyacetone phosphate (DHAP), and ammonia hydrolyzed from glutamine by a complexed glutaminase. Of the three active sites of deoxyxylulose 5-phosphate (DXP)-independent PLP synthase (Pdx1), the R5P isomerization site has been assigned, but the sites for DHAP isomerization and PLP formation remain unknown. Here, we present the crystal structures of yeast Pdx1/Snz1, in apo-, glyceraldehyde 3-phosphate (G3P)- and PLP-bound forms, at 2.30, 1.80, and 2.20 A, respectively. Structural and biochemical analysis enabled us to assign the PLP-formation site, a G3P-binding site and a G3P-transfer site. We propose a putative catalytic mechanism for Pdx1/Snz1 in which R5P and DHAP are isomerized at two distinct sites and transferred along well-defined routes to a final destination for PLP synthesis. | ||
| - | + | Structural insights into the catalytic mechanism of the yeast pyridoxal 5-phosphate synthase Snz1.,Zhang X, Teng YB, Liu JP, He YX, Zhou K, Chen Y, Zhou CZ Biochem J. 2010 Oct 5. PMID:20919991<ref>PMID:20919991</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3o06" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
| + | [[Category: Hu HX]] | ||
| + | [[Category: Teng YB]] | ||
| + | [[Category: Zhang X]] | ||
| + | [[Category: Zhou CZ]] | ||
Current revision
Crystal Structure of yeast pyridoxal 5-phosphate synthase Snz1
| |||||||||||
