3re1
From Proteopedia
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| - | + | ==Crystal structure of uroporphyrinogen III synthase from Pseudomonas syringae pv. tomato DC3000== | |
| - | + | <StructureSection load='3re1' size='340' side='right' caption='[[3re1]], [[Resolution|resolution]] 2.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3re1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._tomato Pseudomonas syringae pv. tomato]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RE1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RE1 FirstGlance]. <br> | ||
| + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hemD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=323 Pseudomonas syringae pv. tomato])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Uroporphyrinogen-III_synthase Uroporphyrinogen-III synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.75 4.2.1.75] </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=3re1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3re1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3re1 RCSB], [http://www.ebi.ac.uk/pdbsum/3re1 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Uroporphyrinogen III synthase (U3S) is one of the key enzymes in the biosynthesis of tetrapyrrole compounds. It catalyzes the cyclization of the linear hydroxymethylbilane (HMB) to uroporphyrinogen III (uro'gen III). We have determined the crystal structure of U3S from Pseudomonas syringae pv. tomato DC3000 (psU3S) at 2.5A resolution by the single wavelength anomalous dispersion (SAD) method. Each psU3S molecule consists of two domains interlinked by a two-stranded antiparallel beta-sheet. The conformation of psU3S is different from its homologous proteins because of the flexibility of the linker between the two domains, which might be related to this enzyme's catalytic properties. Based on mutation and activity analysis, a key residue, Arg219, was found to be important for the catalytic activity of psU3S. Mutation of Arg219 to Ala caused a decrease in enzymatic activity to about 25% that of the wild type enzyme. Our results provide the structural basis and biochemical evidence to further elucidate the catalytic mechanism of U3S. | ||
| - | + | Crystal structure of uroporphyrinogen III synthase from Pseudomonas syringae pv. tomato DC3000.,Peng S, Zhang H, Gao Y, Pan X, Cao P, Li M, Chang W Biochem Biophys Res Commun. 2011 May 20;408(4):576-81. Epub 2011 Apr 19. PMID:21527255<ref>PMID:21527255</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Pseudomonas syringae pv. tomato]] | [[Category: Pseudomonas syringae pv. tomato]] | ||
[[Category: Uroporphyrinogen-III synthase]] | [[Category: Uroporphyrinogen-III synthase]] | ||
| - | [[Category: Chang, W R | + | [[Category: Chang, W R]] |
| - | [[Category: Li, M | + | [[Category: Li, M]] |
| - | [[Category: Peng, S X | + | [[Category: Peng, S X]] |
[[Category: Hemd-like family]] | [[Category: Hemd-like family]] | ||
[[Category: Hmb]] | [[Category: Hmb]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
[[Category: Uroporphyrinogen iii synthase]] | [[Category: Uroporphyrinogen iii synthase]] | ||
Revision as of 10:44, 19 December 2014
Crystal structure of uroporphyrinogen III synthase from Pseudomonas syringae pv. tomato DC3000
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