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Met repressor
From Proteopedia
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[[Taylor met repressor]]<br /> | [[Taylor met repressor]]<br /> | ||
[[Joe Granger Methionine Repressor: Escherichia coli]]. | [[Joe Granger Methionine Repressor: Escherichia coli]]. | ||
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| + | == Structural highlights == | ||
| + | SAM binds to MR in a hydrophobic pocket between 2 monomers<ref>PMID:10986458</ref>. | ||
== 3D Structures of Met repressor == | == 3D Structures of Met repressor == | ||
Revision as of 06:59, 21 April 2016
Contents |
Function
Met repressor (MR) interacts with the DNA operator (Met box) repressing methionine synthesis. The co-repressor of MR is S-adenosyl methionine (SAM) which is a product of methionine synthesis. Binding of SAM to MR increases the repressor affinity to the DNA thus halting methionine synthesis[1]. For additional details see
Taylor met repressor
Joe Granger Methionine Repressor: Escherichia coli.
Structural highlights
SAM binds to MR in a hydrophobic pocket between 2 monomers[2].
3D Structures of Met repressor
Updated on 21-April-2016
1cmb – EcMR – Escherichia coli
1mjk – EcMR (mutant)
1cma – EcMR + DNA
1mjm – EcMR (mutant) + DNA
1cmc – EcMR + SAM
1mjl, 1mjp – EcMR (mutant) + SAM
1mj2, 1mjo, 1mjq – EcMR (mutant) + SAM + DNA
References
- ↑ Somers WS, Rafferty JB, Phillips K, Strathdee S, He YY, McNally T, Manfield I, Navratil O, Old IG, Saint-Girons I, et al.. The Met repressor-operator complex: DNA recognition by beta-strands. Ann N Y Acad Sci. 1994 Jul 29;726:105-17. PMID:8092669
- ↑ Garvie CW, Phillips SE. Direct and indirect readout in mutant Met repressor-operator complexes. Structure. 2000 Sep 15;8(9):905-14. PMID:10986458
