1snn: Difference between revisions

Revision as of 16:03, 21 February 2008

3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii

OverviewOverview

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 centre has recently been determined at 1.7 A resolution. The enzyme converts ribulose 5-phosphate into 3,4-dihydroxy-2-butanone 4-phosphate, while its C4 atom is released as formate. The resulting four-carbon body supplies all eight C atoms for the xylene moiety of riboflavin. Three of the four hydroxyl groups of ribulose 5-phosphate were coordinated by the metal ions. Based on crystallographic refinement, the metals were assigned as zinc and calcium, which were present in the crystallization buffer. Neither metal supports the enzymatic reaction. In the present study, the correctness of this assignment is assessed using anomalous diffraction data collected at the high-energy side of the zinc absorption edge (lambda = 1.2823 A). Only the three tentative zinc ions give strong peaks in an anomalous difference Fourier map (>20sigma), whereas the four tentative calcium ions do not show anomalous signals above the noise level. These results confirm the initial assignment. In addition, the resolution was improved to 1.55 A.

About this StructureAbout this Structure

1SNN is a Single protein structure of sequence from Methanocaldococcus jannaschii with , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Metal sites in 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with the substrate ribulose 5-phosphate., Steinbacher S, Schiffmann S, Bacher A, Fischer M, Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1338-40. Epub 2004, Jun 22. PMID:15213409

Page seeded by OCA on Thu Feb 21 15:03:23 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1snn.gif|left|200px]]<br /><applet load="1snn" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1snn.gif|left|200px]]<br /><applet load="1snn" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1snn, resolution 1.55&Aring;" />
 '''3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii'''<br />
 ==Overview==
-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 centre has recently been determined at 1.7 A resolution. The, enzyme converts ribulose 5-phosphate into 3,4-dihydroxy-2-butanone, 4-phosphate, while its C4 atom is released as formate. The resulting, four-carbon body supplies all eight C atoms for the xylene moiety of, riboflavin. Three of the four hydroxyl groups of ribulose 5-phosphate were, coordinated by the metal ions. Based on crystallographic refinement, the, metals were assigned as zinc and calcium, which were present in the, crystallization buffer. Neither metal supports the enzymatic reaction. In, the present study, the correctness of this assignment is assessed using, anomalous diffraction data collected at the high-energy side of the zinc, absorption edge (lambda = 1.2823 A). Only the three tentative zinc ions, give strong peaks in an anomalous difference Fourier map (&gt;20sigma), whereas the four tentative calcium ions do not show anomalous signals, above the noise level. These results confirm the initial assignment. In, addition, the resolution was improved to 1.55 A.
+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 centre has recently been determined at 1.7 A resolution. The enzyme converts ribulose 5-phosphate into 3,4-dihydroxy-2-butanone 4-phosphate, while its C4 atom is released as formate. The resulting four-carbon body supplies all eight C atoms for the xylene moiety of riboflavin. Three of the four hydroxyl groups of ribulose 5-phosphate were coordinated by the metal ions. Based on crystallographic refinement, the metals were assigned as zinc and calcium, which were present in the crystallization buffer. Neither metal supports the enzymatic reaction. In the present study, the correctness of this assignment is assessed using anomalous diffraction data collected at the high-energy side of the zinc absorption edge (lambda = 1.2823 A). Only the three tentative zinc ions give strong peaks in an anomalous difference Fourier map (&gt;20sigma), whereas the four tentative calcium ions do not show anomalous signals above the noise level. These results confirm the initial assignment. In addition, the resolution was improved to 1.55 A.
 ==About this Structure==
-SNN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with 5RP, ZN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SNN OCA].
+SNN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with <scene name='pdbligand=5RP:'>5RP</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SNN OCA].
 ==Reference==
@@ Line 23: / Line 23: @@
 [[Category: riboflavin biosynthesis]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:30:49 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:03:23 2008''