1pvw
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1pvw.jpg|left|200px]] | [[Image:1pvw.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1pvw", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1pvw| PDB=1pvw | SCENE= }} | |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''3,4-dihydroxy-2-butanone 4-phosphate synthase from M. jannaschii''' | '''3,4-dihydroxy-2-butanone 4-phosphate synthase from M. jannaschii''' | ||
| Line 31: | Line 28: | ||
[[Category: Schiffmann, S.]] | [[Category: Schiffmann, S.]] | ||
[[Category: Steinbacher, S.]] | [[Category: Steinbacher, S.]] | ||
| - | [[Category: | + | [[Category: Riboflavin biosynthesis]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:32:50 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 02:32, 3 May 2008
3,4-dihydroxy-2-butanone 4-phosphate synthase from M. jannaschii
Overview
Skeletal rearrangements of carbohydrates are crucial for many biosynthetic pathways. In riboflavin biosynthesis ribulose 5-phosphate is converted into 3,4-dihydroxy-2-butanone 4-phosphate while its C4 atom is released as formate in a sequence of metal-dependent reactions. Here, we present the crystal structure of Methanococcus jannaschii 3,4-dihydroxy-2-butanone 4-phosphate synthase in complex with the substrate ribulose 5-phosphate at a dimetal center presumably consisting of non-catalytic zinc and calcium ions at 1.7-A resolution. The carbonyl group (O2) and two out of three free hydroxyl groups (OH3 and OH4) of the substrate are metal-coordinated. We correlate previous mutational studies on this enzyme with the present structural results. Residues of the first coordination sphere involved in metal binding are indispensable for catalytic activity. Only Glu-185 of the second coordination sphere cannot be replaced without complete loss of activity. It contacts the C3 hydrogen atom directly and probably initiates enediol formation in concert with both metal ions to start the reaction sequence. Mechanistic similarities to Rubisco acting on the similar substrate ribulose 1,5-diphosphate in carbon dioxide fixation as well as other carbohydrate (reducto-) isomerases are discussed.
About this Structure
1PVW is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.
Reference
Structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with divalent metal ions and the substrate ribulose 5-phosphate: implications for the catalytic mechanism., Steinbacher S, Schiffmann S, Richter G, Huber R, Bacher A, Fischer M, J Biol Chem. 2003 Oct 24;278(43):42256-65. Epub 2003 Aug 6. PMID:12904291 Page seeded by OCA on Sat May 3 05:32:50 2008
