1gpu
From Proteopedia
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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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| - | The line below this paragraph, {{ABSTRACT_PUBMED_11773632}}, adds the Publication Abstract to the page | ||
| - | (as it appears on PubMed at http://www.pubmed.gov), where 11773632 is the PubMed ID number. | ||
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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]. |
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| + | ==See Also== | ||
| + | *[[Transketolase|Transketolase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <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
Contents |
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
- 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
- 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
- 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
- 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
- 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:http://dx.doi.org/10.1006/jmbi.1994.1299
- 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:http://dx.doi.org/10.1074/jbc.M300339200
