1v1q

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[[Category: primosome]]
[[Category: primosome]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:36:20 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:18:27 2007''

Revision as of 14:13, 30 October 2007


1v1q, resolution 2.10Å

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CRYSTAL STRUCTURE OF PRIB- A PRIMOSOMAL DNA REPLICATION PROTEIN OF ESCHERICHIA COLI

Overview

PriB is one of the Escherichia coli varphiX-type primosome proteins that, are required for assembly of the primosome, a mobile multi-enzyme complex, responsible for the initiation of DNA replication. Here we report the, crystal structure of the E. coli PriB at 2.1 A resolution by, multi-wavelength anomalous diffraction using a mercury derivative. The, polypeptide chain of PriB is structurally similar to that of, single-stranded DNA-binding protein (SSB). However, the biological unit of, PriB is a dimer, not a homotetramer like SSB. Electrophoretic mobility, shift assays demonstrated that PriB binds single-stranded DNA and, single-stranded RNA with comparable affinity. We also show that PriB binds, single-stranded DNA with certain base preferences. Based on the PriB, structural information ... [(full description)]

About this Structure

1V1Q is a [Single protein] structure of sequence from [Escherichia coli] with CYS and CYS as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal structure of PriB, a primosomal DNA replication protein of Escherichia coli., Liu JH, Chang TW, Huang CY, Chen SU, Wu HN, Chang MC, Hsiao CD, J Biol Chem. 2004 Nov 26;279(48):50465-71. Epub 2004 Sep 21. PMID:15383524

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