4i64
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
- | + | {{STRUCTURE_4i64| PDB=4i64 | SCENE= }} | |
+ | ===3-hydroxy-3-methylglutaryl Coenzyme A reductase from Pseudomonas mevalonii, a high resolution native structure=== | ||
+ | {{ABSTRACT_PUBMED_23802607}} | ||
- | + | ==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. | ||
- | + | ==About this Structure== | |
+ | [[4i64]] 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=4I64 OCA]. | ||
- | + | ==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 W.Burgner.]] | ||
+ | [[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
Contents |
3-hydroxy-3-methylglutaryl Coenzyme A reductase from Pseudomonas mevalonii, a high resolution native structure
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
4i64 is a 2 chain structure with sequence from Pseudomonas mevalonii. Full crystallographic information is available from OCA.
Reference
- 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