1z6r
From Proteopedia
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'''Crystal structure of Mlc from Escherichia coli''' | '''Crystal structure of Mlc from Escherichia coli''' | ||
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[[Category: Seitz, S.]] | [[Category: Seitz, S.]] | ||
[[Category: Welte, W.]] | [[Category: Welte, W.]] | ||
- | [[Category: | + | [[Category: Dna binding protein]] |
- | [[Category: | + | [[Category: Helix-turn-helix]] |
- | [[Category: | + | [[Category: Metalloprotein]] |
- | [[Category: | + | [[Category: Phosphotransferase system]] |
- | [[Category: | + | [[Category: Rok family protein]] |
- | [[Category: | + | [[Category: Transcriptional repressor]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:14:47 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 14:14, 3 May 2008
Crystal structure of Mlc from Escherichia coli
Overview
Mlc from Escherichia coli is a transcriptional repressor controlling the expression of a number of genes encoding enzymes of the phosphotransferase system (PTS), including ptsG and manXYZ, the specific enzyme II for glucose and mannose PTS transporters. In addition, Mlc controls the transcription of malT, the gene of the global activator of the mal regulon. The inactivation of Mlc as a repressor is mediated by binding to an actively transporting PtsG (EIICB(Glc)). Here we report the crystal structure of Mlc at 2.7 A resolution representing the first described structure of an ROK (repressors, open reading frames, and kinases) family protein. Mlc forms stable dimers thus explaining its binding affinity to palindromic operator sites. The N-terminal helix-turn-helix domain of Mlc is stabilized by the amphipathic C-terminal helix implicated earlier in EIICB(Glc) binding. Furthermore, the structure revealed a metal-binding site within the cysteine-rich ROK consensus motif that coordinates a structurally important zinc ion. A strongly reduced repressor activity was observed when two of the zinc-coordinating cysteine residues were exchanged against serine or alanine, demonstrating the role of zinc in Mlc-mediated repressor function. The structures of a putative fructokinase from Bacillus subtilis, the glucokinase from Escherichia coli, and a glucomannokinase from Arthrobacter sp. showed high structural homology to the ROK family part of Mlc.
About this Structure
1Z6R is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The crystal structure of Mlc, a global regulator of sugar metabolism in Escherichia coli., Schiefner A, Gerber K, Seitz S, Welte W, Diederichs K, Boos W, J Biol Chem. 2005 Aug 12;280(32):29073-9. Epub 2005 Jun 1. PMID:15929984 Page seeded by OCA on Sat May 3 17:14:47 2008