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1ofp
From Proteopedia
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[[Image:1ofp.png|left|200px]] | [[Image:1ofp.png|left|200px]] | ||
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{{STRUCTURE_1ofp| PDB=1ofp | SCENE= }} | {{STRUCTURE_1ofp| PDB=1ofp | SCENE= }} | ||
===CRYSTAL STRUCTURE OF THE TYROSINE-REGULATED 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-PHOSPHATE SYNTHASE FROM SACCHAROMYCES CEREVISIAE=== | ===CRYSTAL STRUCTURE OF THE TYROSINE-REGULATED 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-PHOSPHATE SYNTHASE FROM SACCHAROMYCES CEREVISIAE=== | ||
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{{ABSTRACT_PUBMED_15019786}} | {{ABSTRACT_PUBMED_15019786}} | ||
==About this Structure== | ==About this Structure== | ||
| - | [[1ofp]] is a 4 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=1OFP OCA]. | + | [[1ofp]] is a 4 chain structure of [[Aldolase]] 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=1OFP OCA]. |
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| + | ==See Also== | ||
| + | *[[Aldolase|Aldolase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:015019786</ref><ref group="xtra">PMID:012540830</ref><references group="xtra"/> |
[[Category: 3-deoxy-7-phosphoheptulonate synthase]] | [[Category: 3-deoxy-7-phosphoheptulonate synthase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
Revision as of 18:59, 26 July 2012
Contents |
CRYSTAL STRUCTURE OF THE TYROSINE-REGULATED 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-PHOSPHATE SYNTHASE FROM SACCHAROMYCES CEREVISIAE
Template:ABSTRACT PUBMED 15019786
About this Structure
1ofp is a 4 chain structure of Aldolase with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
See Also
Reference
- Konig V, Pfeil A, Braus GH, Schneider TR. Substrate and metal complexes of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Saccharomyces cerevisiae provide new insights into the catalytic mechanism. J Mol Biol. 2004 Mar 26;337(3):675-90. PMID:15019786 doi:http://dx.doi.org/10.1016/j.jmb.2004.01.055
- Hartmann M, Schneider TR, Pfeil A, Heinrich G, Lipscomb WN, Braus GH. Evolution of feedback-inhibited beta /alpha barrel isoenzymes by gene duplication and a single mutation. Proc Natl Acad Sci U S A. 2003 Feb 4;100(3):862-7. Epub 2003 Jan 22. PMID:12540830 doi:10.1073/pnas.0337566100
