Joe Granger Methionine Repressor: Escherichia coli

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-	BKT Assistant Professor of Chemistry at Wabash College	+	[[Image:1cma.png|left|200px]]
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		+	{{STRUCTURE_1cma| PDB=1cma | SCENE= }}
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		+	===MET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE===
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		+	{{The crystal structure of the met repressor-operator complex shows two dimeric repressor molecules bound to adjacent sites 8 base pairs apart on an 18-base-pair DNA fragment. Sequence specificity is achieved by insertion of double-stranded antiparallel protein beta-ribbons into the major groove of B-form DNA, with direct hydrogen-bonding between amino-acid side chains and the base pairs. The repressor also recognizes sequence-dependent distortion or flexibility of the operator phosphate backbone, conferring specificity even for inaccessible base pairs. }}
		+
		+	==About this Structure==
		+	[[1cma]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMA OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:001406951</ref><references group="xtra"/>
		+	[[Category: Escherichia coli]]
		+	[[Category: Phillips, S E.V.]]
		+	[[Category: Somers, W S.]]
		+	[[Category: Double helix]]
		+	[[Category: Protein-dna complex]]
		+	[[Category: Transcription-dna complex]]

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Revision as of 00:03, 8 November 2012

spinqualitylabelsall models PDB ID 1cma Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1cma, resolution 2.80Å ()
Ligands:
Structural annotation: Resources: CATH : 1Cmaa00, 1Cmab00 InterPro : Ipr010985, Ipr002084 Pfam : PF01340 SCOP : d1cmaa_, d1cmab_ UniProt : P0A8U6
Functional annotation: Cellular component: cytoplasm Biological process: methionine metabolic process amino acid biosynthetic process negative regulation of transcription, DNA-dependent transcription regulation of transcription, DNA-dependent regulation of transcription methionine biosynthetic process Molecular function: DNA binding transcription repressor activity transcription factor activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

MET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE

{{The crystal structure of the met repressor-operator complex shows two dimeric repressor molecules bound to adjacent sites 8 base pairs apart on an 18-base-pair DNA fragment. Sequence specificity is achieved by insertion of double-stranded antiparallel protein beta-ribbons into the major groove of B-form DNA, with direct hydrogen-bonding between amino-acid side chains and the base pairs. The repressor also recognizes sequence-dependent distortion or flexibility of the operator phosphate backbone, conferring specificity even for inaccessible base pairs. }}

About this Structure

1cma is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

• Somers WS, Phillips SE. Crystal structure of the met repressor-operator complex at 2.8 A resolution reveals DNA recognition by beta-strands. Nature. 1992 Oct 1;359(6394):387-93. PMID:1406951 doi:http://dx.doi.org/10.1038/359387a0