4JOM

Structure of E. coli Pol III 3mPHP mutant

Summary for 4JOM

• Entry DOI: 10.2210/pdb4jom/pdb
• Related: 2HNH
• Descriptor: DNA polymerase III subunit alpha, PHOSPHATE ION, ZINC ION, ... (5 entities in total)
• Functional Keywords: dna polymerase, dna binding, dntp binding, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P10443
• Total number of polymer chains: 1
• Total formula weight: 103097.02

Authors

Barros, T.,Guenther, J.,Kelch, B.,Anaya, J.,Prabhakar, A.,O'Donnell, M.,Kuriyan, J.,Lamers, M.H. (deposition date: 2013-03-18, release date: 2013-05-29, Last modification date: 2023-09-20)

Primary citation

Barros, T.,Guenther, J.,Kelch, B.,Anaya, J.,Prabhakar, A.,O Donnell, M.,Kuriyan, J.,Lamers, M.H.
A structural role for the PHP domain in E. coli DNA polymerase III.
Bmc Struct.Biol., 13:8-8, 2013

PubMed Abstract: In addition to the core catalytic machinery, bacterial replicative DNA polymerases contain a Polymerase and Histidinol Phosphatase (PHP) domain whose function is not entirely understood. The PHP domains of some bacterial replicases are active metal-dependent nucleases that may play a role in proofreading. In E. coli DNA polymerase III, however, the PHP domain has lost several metal-coordinating residues and is likely to be catalytically inactive.

PubMed: 23672456
DOI: 10.1186/1472-6807-13-8

Experimental method

X-RAY DIFFRACTION (2.9 Å)