1cma: Difference between revisions

Revision as of 20:56, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

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-METHIONINEMET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE

Template:ABSTRACT PUBMED 1406951

About this StructureAbout this Structure

1CMA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Mon Jun 30 20:56:37 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-==Overview==
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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.
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