2vu2
From Proteopedia
(Difference between revisions)
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===BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX WITH S-PANTETHEINE-11-PIVALATE.=== | ===BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX WITH S-PANTETHEINE-11-PIVALATE.=== | ||
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+ | <!-- | ||
+ | The line below this paragraph, {{ABSTRACT_PUBMED_19016856}}, adds the Publication Abstract to the page | ||
+ | (as it appears on PubMed at http://www.pubmed.gov), where 19016856 is the PubMed ID number. | ||
+ | --> | ||
+ | {{ABSTRACT_PUBMED_19016856}} | ||
==About this Structure== | ==About this Structure== | ||
- | 2VU2 is a | + | 2VU2 is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Zoogloea_ramigera Zoogloea ramigera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VU2 OCA]. |
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+ | ==Reference== | ||
+ | The sulfur atoms of the substrate CoA and the catalytic cysteine are required for a productive mode of substrate binding in bacterial biosynthetic thiolase, a thioester-dependent enzyme., Merilainen G, Schmitz W, Wierenga RK, Kursula P, FEBS J. 2008 Dec;275(24):6136-48. Epub 2008 Nov 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/19016856 19016856] | ||
[[Category: Acetyl-CoA C-acetyltransferase]] | [[Category: Acetyl-CoA C-acetyltransferase]] | ||
- | [[Category: Single protein]] | ||
[[Category: Zoogloea ramigera]] | [[Category: Zoogloea ramigera]] | ||
[[Category: Kursula, P.]] | [[Category: Kursula, P.]] | ||
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[[Category: Transferase]] | [[Category: Transferase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 10 15:21:30 2008'' |
Revision as of 13:21, 10 December 2008
BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX WITH S-PANTETHEINE-11-PIVALATE.
Template:ABSTRACT PUBMED 19016856
About this Structure
2VU2 is a 4 chains structure of sequences from Zoogloea ramigera. Full crystallographic information is available from OCA.
Reference
The sulfur atoms of the substrate CoA and the catalytic cysteine are required for a productive mode of substrate binding in bacterial biosynthetic thiolase, a thioester-dependent enzyme., Merilainen G, Schmitz W, Wierenga RK, Kursula P, FEBS J. 2008 Dec;275(24):6136-48. Epub 2008 Nov 1. PMID:19016856
Page seeded by OCA on Wed Dec 10 15:21:30 2008