1kaw

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{{STRUCTURE_1kaw| PDB=1kaw | SCENE= }}
{{STRUCTURE_1kaw| PDB=1kaw | SCENE= }}
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'''STRUCTURE OF SINGLE STRANDED DNA BINDING PROTEIN (SSB)'''
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===STRUCTURE OF SINGLE STRANDED DNA BINDING PROTEIN (SSB)===
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==Overview==
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The crystal structure of the tetrameric DNA-binding domain of the single-stranded DNA binding protein from Escherichia coli was determined at a resolution of 2.9 A using multiwavelength anomalous dispersion. Each monomer in the tetramer is topologically similar to an oligomer-binding fold. Two monomers each contribute three beta-strands to a single six-stranded beta-sheet to form a dimer. Two dimer-dimer interfaces are observed within the crystal. One of these stabilizes the tetramer in solution. The other interface promotes a superhelical structure within the crystal that may reflect tetramer-tetramer interactions involved in the positive cooperative binding of the single-stranded DNA-binding protein to single-stranded DNA.
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(as it appears on PubMed at http://www.pubmed.gov), where 9192620 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9192620}}
==About this Structure==
==About this Structure==
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[[Category: Single stranded dna binding protein]]
[[Category: Single stranded dna binding protein]]
[[Category: Ssb]]
[[Category: Ssb]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:03:18 2008''

Revision as of 07:03, 2 July 2008

Image:1kaw.png

Template:STRUCTURE 1kaw

STRUCTURE OF SINGLE STRANDED DNA BINDING PROTEIN (SSB)

Template:ABSTRACT PUBMED 9192620

About this Structure

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

Reference

Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-A resolution., Raghunathan S, Ricard CS, Lohman TM, Waksman G, Proc Natl Acad Sci U S A. 1997 Jun 24;94(13):6652-7. PMID:9192620

Page seeded by OCA on Wed Jul 2 10:03:18 2008

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