4i6y: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4i6y|  PDB=4i6y  |  SCENE=  }}
===3-hydroxy-3-methyl (HMG) Coenzyme A Reductase bound to R-Mevalonate===
{{ABSTRACT_PUBMED_23802607}}


The entry 4i6y is ON HOLD  until Paper Publication
==Function==
[[http://www.uniprot.org/uniprot/MVAA_PSEMV MVAA_PSEMV]] P.mevalonii can use mevalonate as sole carbon source. With this enzyme mevalonate is deacetylated to HMG-CoA.


Authors: Steussy, C.N., Stauffacher, C.V., Schmidt, T., Burgner II, J.W, Rodwell, V.W., Wrensford, L.V., Critchelow, C.J., Min, J.
==About this Structure==
[[4i6y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_mevalonii Pseudomonas mevalonii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I6Y OCA].  


Description: 3-hydroxy-3-methyl (HMG) Coenzyme A Reductase bound to R-Mevalonate
==Reference==
<ref group="xtra">PMID:023802607</ref><references group="xtra"/><references/>
[[Category: Hydroxymethylglutaryl-CoA reductase]]
[[Category: Pseudomonas mevalonii]]
[[Category: Critchelow, C J.]]
[[Category: II, J WBurgner.]]
[[Category: Min, J.]]
[[Category: Rodwell, V W.]]
[[Category: Schmidt, T.]]
[[Category: Stauffacher, C V.]]
[[Category: Steussy, C N.]]
[[Category: Wrensford, L V.]]
[[Category: Oxidoreductase]]

Revision as of 04:58, 18 July 2013

Template:STRUCTURE 4i6y

3-hydroxy-3-methyl (HMG) Coenzyme A Reductase bound to R-Mevalonate

Template:ABSTRACT PUBMED 23802607

Function

[MVAA_PSEMV] P.mevalonii can use mevalonate as sole carbon source. With this enzyme mevalonate is deacetylated to HMG-CoA.

About this Structure

4i6y is a 2 chain structure with sequence from Pseudomonas mevalonii. Full crystallographic information is available from OCA.

Reference

  1. Steussy CN, Critchelow CJ, Schmidt TJ, Min JK, Wrensford LV, Burgner JW, Rodwell VW, Stauffacher CV. A novel role for CoA during hydride transfer in 3-hydroxy-3-methylglutaryl-coenzyme A reductase. Biochemistry. 2013 Jun 26. PMID:23802607 doi:10.1021/bi400335g

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