1snn: Difference between revisions

Revision as of 10:12, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1snn.png

Template:STRUCTURE 1snn

3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii

Template:ABSTRACT PUBMED 15213409

About this StructureAbout this Structure

1SNN is a Single protein structure of sequence from Methanocaldococcus jannaschii. 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

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

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OCA

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-[[Image:1snn.gif|left|200px]]
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 {{STRUCTURE_1snn|  PDB=1snn  |  SCENE=  }}
-'''3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii'''
+===3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii===
-==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 line below this paragraph, {{ABSTRACT_PUBMED_15213409}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15213409 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15213409}}
 ==About this Structure==
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 ==Reference==
 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:[http://www.ncbi.nlm.nih.gov/pubmed/15213409 15213409]
+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:[http://www.ncbi.nlm.nih.gov/pubmed/12904291 12904291]
 [[Category: Methanocaldococcus jannaschii]]
 [[Category: Single protein]]
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 [[Category: Steinbacher, S.]]
 [[Category: Riboflavin biosynthesis]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:55:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:12:13 2008''