1gpu: Difference between revisions

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[[Image:1gpu.png|left|200px]]
[[Image:1gpu.png|left|200px]]


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{{STRUCTURE_1gpu|  PDB=1gpu  |  SCENE=  }}  
{{STRUCTURE_1gpu|  PDB=1gpu  |  SCENE=  }}  


===TRANSKETOLASE COMPLEX WITH REACTION INTERMEDIATE===
===TRANSKETOLASE COMPLEX WITH REACTION INTERMEDIATE===


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{{ABSTRACT_PUBMED_11773632}}
{{ABSTRACT_PUBMED_11773632}}


==About this Structure==
==About this Structure==
[[1gpu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPU OCA].  
[[1gpu]] is a 2 chain structure of [[Transketolase]] with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPU OCA].  
 
==See Also==
*[[Transketolase|Transketolase]]


==Reference==
==Reference==
<ref group="xtra">PMID:11773632</ref><ref group="xtra">PMID:9398292</ref><ref group="xtra">PMID:9119035</ref><ref group="xtra">PMID:8974393</ref><ref group="xtra">PMID:8176731</ref><references group="xtra"/>
<ref group="xtra">PMID:011773632</ref><ref group="xtra">PMID:009398292</ref><ref group="xtra">PMID:009119035</ref><ref group="xtra">PMID:008974393</ref><ref group="xtra">PMID:008176731</ref><ref group="xtra">PMID:012651851</ref><references group="xtra"/>
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Transketolase]]
[[Category: Transketolase]]

Revision as of 20:14, 26 July 2012

File:1gpu.png

Template:STRUCTURE 1gpu

TRANSKETOLASE COMPLEX WITH REACTION INTERMEDIATE

Template:ABSTRACT PUBMED 11773632

About this Structure

1gpu is a 2 chain structure of Transketolase with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

See Also

Reference

  1. Fiedler E, Thorell S, Sandalova T, Golbik R, Konig S, Schneider G. Snapshot of a key intermediate in enzymatic thiamin catalysis: crystal structure of the alpha-carbanion of (alpha,beta-dihydroxyethyl)-thiamin diphosphate in the active site of transketolase from Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):591-5. Epub 2002 Jan 2. PMID:11773632 doi:10.1073/pnas.022510999
  2. Wikner C, Nilsson U, Meshalkina L, Udekwu C, Lindqvist Y, Schneider G. Identification of catalytically important residues in yeast transketolase. Biochemistry. 1997 Dec 16;36(50):15643-9. PMID:9398292 doi:10.1021/bi971606b
  3. Meshalkina L, Nilsson U, Wikner C, Kostikowa T, Schneider G. Examination of the thiamin diphosphate binding site in yeast transketolase by site-directed mutagenesis. Eur J Biochem. 1997 Mar 1;244(2):646-52. PMID:9119035
  4. Kern D, Kern G, Neef H, Tittmann K, Killenberg-Jabs M, Wikner C, Schneider G, Hubner G. How thiamine diphosphate is activated in enzymes. Science. 1997 Jan 3;275(5296):67-70. PMID:8974393
  5. Nikkola M, Lindqvist Y, Schneider G. Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 A resolution. J Mol Biol. 1994 May 6;238(3):387-404. PMID:8176731 doi:https://dx.doi.org/10.1006/jmbi.1994.1299
  6. Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS. Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase. J Biol Chem. 2003 Jun 6;278(23):21240-6. Epub 2003 Mar 21. PMID:12651851 doi:https://dx.doi.org/10.1074/jbc.M300339200

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